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Curr Opin Cell Biol 21:575–581\nMathivanan S, Ji H, Simpson RJ (2010) Exosomes: extracellular organelles important in intercellular communication. J Proteom 73:1907–1920\nGross JC, Chaudhary V, Bartscherer K, Boutros M (2012) Active Wnt proteins are secreted on exosomes. Nat Cell Biol 14:1036\nSato-Kuwabara Y, Melo SA, Soares FA, Calin GA (2015) The fusion of two worlds: Non-coding RNAs and extracellular vesicles-diagnostic and therapeutic implications. Int J Oncol 46:17–27\nSrikanthan S, Li W, Silverstein RL, McIntyre TM (2014) Exosome poly-ubiquitin inhibits platelet activation, downregulates CD 36 and inhibits pro-atherothombotic cellular functions. J Thromb Haemost 12:1906–1917\nTkach M, Théry C (2016) Communication by extracellular vesicles: where we are and where we need to go. Cell 164:1226–1232\nBoulanger CM, Loyer X, Rautou P-E, Amabile N (2017) Extracellular vesicles in coronary artery disease. Nat Rev Cardiol 14:259\nBartel DP (2004) MicroRNAs: genomics, biogenesis, mechanism, and function. Cell 116:281–297\nHe L, Hannon GJ (2004) MicroRNAs: small RNAs with a big role in gene regulation. Nat Rev Genet 5:522–531\nZhang J, Li S, Li L, Li M, Guo C, Yao J, Mi S (2015) Exosome and exosomal microRNA: trafficking, sorting, and function. Genom Proteom Bioinf 13:17–24\nXu X, Subbarao K, Cox NJ, Guo Y (1999) Genetic characterization of the pathogenic influenza A\u002FGoose\u002FGuangdong\u002F1\u002F96 (H5N1) virus: similarity of its hemagglutinin gene to those of H5N1 viruses from the 1997 outbreaks in Hong Kong. Virology 261:15–19\nKullman G (2008) Protecting poultry workers from avian influenza (bird Flu). Department of Health and Human Services, Cincinnati\nWorld Health Organization. https:\u002F\u002Fwww.who.int\u002Finfluenza\u002Fhuman_animal_interface\u002Fen\u002F. Accessed 5 Sept 2020\nVeerman RE, Akpinar GG, Eldh M, Gabrielsson S (2019) Immune cell-derived extracellular vesicles–functions and therapeutic applications. Trends Mol Med 25:382–394\nMoula N, Dang PK, Farnir F, Ton VD, Binh DV, Leroy P, Antoine-Moussiaux N (2011) The Ri chicken breed and livelihoods in North Vietnam: characterization and prospects. J Agr Rural Dev Trop 112:57–69\nSeyama T, Ko J, Ohe M, Sasaoka N, Okada A, Gomi H, Yoneda A, Ueda J, Nishibori M, Okamoto S (2006) Population research of genetic polymorphism at amino acid position 631 in chicken Mx protein with differential antiviral activity. Biochem Genet 44:432–443\nBerlin S, Qu L, Li X, Yang N, Ellegren H (2008) Positive diversifying selection in avian Mx genes. Immunogenetics 60:689\nSironi L, Williams JL, Moreno-Martin AM, Ramelli P, Stella A, Jianlin H, Weigend S, Lombardi G, Cordioli P, Mariani P (2008) Susceptibility of different chicken lines to H7N1 highly pathogenic avian influenza virus and the role of Mx gene polymorphism coding amino acid position 631. Virology 380:152–156\nKaufman J (1999) Co-evolving genes in MHC haplotypes: the\" rule\" for nonmammalian vertebrates? Immunogenetics 50:228–236\nMiller MM, Bacon LD, Hala K, Hunt HD, Ewald SJ, Kaufman J, Zoorob R, Briles WE (2004) 2004 Nomenclature for the chicken major histocompatibility (B and Y) complex. Immunogenetics 56:261–279\nMiller MM, Taylor RL Jr (2016) Brief review of the chicken major histocompatibility complex: the genes, their distribution on chromosome 16, and their contributions to disease resistance. Poult Sci 95:375–392\nEwald S, Ye X, Avendano S, McLeod S, Lamont S, Dekkers J (2007) Associations of BF2 alleles with antibody titres and production traits in commercial pure line broiler chickens. Anim Genet 38:174–176\nBoonyanuwat K, Thummabutra S, Sookmanee N, Vatchavalkhu V, Siripholvat V (2006) Influences of major histocompatibility complex class I haplotypes on avian influenza virus disease traits in Thai indigenous chickens. Anim Sci 77:285–289\nHuprikar J, Rabinowitz S (1980) A simplified plaque assay for influenza viruses in Madin-Darby kidney (MDCK) cells. J Virol Methods 1:117–120\nHong Y, Lee J, Vu TH, Lee S, Lillehoj HS, Hong YH (2020) Immunomodulatory effects of avian β-defensin 5 in chicken macrophage cell line. Res Vet Sci 132:81–87\nFastQC v0.11.7. http:\u002F\u002Fwww.bioinformatics.babraham.ac.uk\u002Fprojects\u002Ffastqc\u002F. Accessed 2 Oct 2019\nCutadapt 1.16. https:\u002F\u002Fcutadapt.readthedocs.org\u002Fen\u002Fstable\u002F. 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J Immunol 182:1088–1098\nTruong AD, Hong Y, Lee J, Lee K, Lillehoj HS, Hong YH (2017) Analysis of MAPK signaling pathway genes in the intestinal mucosal layer of necrotic eenteritis-afflicted two inbred chicken lines. Korean J Poult Sci 44:199–209\nXing Z, Cardona CJ, Anunciacion J, Adams S, Dao N (2010) Roles of the ERK MAPK in the regulation of proinflammatory and apoptotic responses in chicken macrophages infected with H9N2 avian influenza virus. J Gen Virol 91:343–351\nLudwig S, Planz O, Pleschka S, Wolff T (2003) Influenza-virus-induced signaling cascades: targets for antiviral therapy? Trends Mol Med 9:46–52\nElbahesh H, Cline T, Baranovich T, Govorkova EA, Schultz-Cherry S, Russell CJ (2014) Novel roles of focal adhesion kinase in cytoplasmic entry and replication of influenza A viruses. J Virol 88:6714–6728\nZhu Z, Qi Y, Ge A, Zhu Y, Xu K, Ji H, Shi Z, Cui L, Zhou M (2014) Comprehensive characterization of serum microRNA profile in response to the emerging avian influenza A (H7N9) virus infection in humans. Viruses 6:1525–1539\nWang Y, Brahmakshatriya V, Zhu H, Lupiani B, Reddy SM, Yoon B-J, Gunaratne PH, Kim JH, Chen R, Wang J (2009) Identification of differentially expressed miRNAs in chicken lung and trachea with avian influenza virus infection by a deep sequencing approach. BMC Genomics 10:512\nWang Y, Brahmakshatriya V, Lupiani B, Reddy SM, Soibam B, Benham AL, Gunaratne P, Liu H-c, Trakooljul N, Ing N (2012) Integrated analysis of microRNA expression and mRNA transcriptome in lungs of avian influenza virus infected broilers. BMC Genomics 13:278\nLam W-Y, Yeung AC-M, Ngai KL-K, Li M-S, To K-F, Tsui SK-W, Chan PK-S (2013) Effect of avian influenza A H5N1 infection on the expression of microRNA-141 in human respiratory epithelial cells. BMC Microbiol 13:104\nbowtie. http:\u002F\u002Fbowtie-bio.sourceforge.net\u002Findex.shtml. Accessed 2 Nov 2019",{"EN":182},"Exosomes are membrane vesicles containing proteins, lipids, DNA, mRNA, and micro RNA (miRNA). Exosomal miRNA from donor cells can regulate the gene expression of recipient cells. Here, Ri chickens were divided into resistant (Mx\u002FA; BF2\u002FB21) and susceptible (Mx\u002FG; BF2\u002FB13) trait by genotyping of Mx and BF2 genes. Then, Ri chickens were infected with H5N1, a highly pathogenic avian influenza virus (HPAIV). Exosomes were purified from blood serum of resistant chickens for small RNA sequencing. Sequencing data were analysed using FastQCv0.11.7, Cutadapt 1.16, miRBase v21, non-coding RNA database, RNAcentral 10.0, and miRDeep2. Differentially expressed miRNAs were determined using statistical methods, including fold-change, exactTest using edgeR, and hierarchical clustering. Target genes were predicted using miRDB. Gene ontology analysis was performed using gProfiler. Twenty miRNAs showed significantly different expression patterns between resistant control and infected chickens. Nine miRNAs were up-regulated and 11 miRNAs were down-regulated in the infected chickens compared with that in the control chickens. In target gene analysis, various immune-related genes, such as cytokines, chemokines, and signalling molecules, were detected. In particular, mitogen-activated protein kinase (MAPK) pathway molecules were highly controlled by differentially expressed miRNAs. The result of qRT-PCR for miRNAs was identical with sequencing data and miRNA expression level was higher in resistant than susceptible chickens. This study will help to better understand the host immune response, particularly exosomal miRNA expression against HPAIV H5N1 and could help to determine biomarkers for disease resistance.",{"EN":184},"Exosomal miRNA profiling from H5N1 avian influenza virus-infected chickens",{"VOID":186},"10.1186\u002Fs13567-021-00892-3","PUBLICATION","VERIFIED","2024-12-05T23:56:35.208+00:00","Auto 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Vu",{"id":212,"sortIndex":111,"researcher":18,"roles":213,"affiliations":214,"properties":225},"10e2be1b-140c-4773-bf1f-3b6393d71f87",[196],[215],{"id":18,"sortIndex":19,"affiliation":216,"properties":18},{"id":217,"createTime":218,"updateTime":219,"relativeEntities":220,"slug":221,"properties":222,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"082edd64-962d-4a3c-8f44-145200e31e52","2024-02-11T09:38:43.288+00:00","2025-06-11T21:11:24.386+00:00",[],"Department-of-Animal-Biotechnology-College-of-Agricultural-and-Life-Sciences-Jeonbuk-National-University-Jeonju-Republic-of-Korea",{"title":223},{"VI":224},"Department of Animal Biotechnology, College of Agricultural and Life Sciences, Jeonbuk National University, Jeonju, Republic of Korea",{"title":226},{"VI":227},"Ki-Duk Song",{"id":229,"sortIndex":19,"researcher":18,"roles":230,"affiliations":231,"properties":237},"c1a32c13-930a-49d3-b23f-73299b985770",[196],[232],{"id":18,"sortIndex":19,"affiliation":233,"properties":18},{"id":200,"createTime":201,"updateTime":202,"relativeEntities":234,"slug":204,"properties":235,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":236},{"VI":207},{"title":238},{"VI":239},"Yeojin Hong",{"id":241,"sortIndex":110,"researcher":18,"roles":242,"affiliations":243,"properties":249},"fb7554ba-04ba-4a9c-ad81-b1d1cace2be4",[196],[244],{"id":18,"sortIndex":19,"affiliation":245,"properties":18},{"id":200,"createTime":201,"updateTime":202,"relativeEntities":246,"slug":204,"properties":247,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":248},{"VI":207},{"title":250},{"VI":251},"Jiae Lee",{"id":253,"sortIndex":109,"researcher":18,"roles":254,"affiliations":255,"properties":264},"c1453327-29a4-47be-a5a8-14fc98cab9cc",[196],[256],{"id":18,"sortIndex":19,"affiliation":257,"properties":18},{"id":258,"createTime":259,"updateTime":259,"relativeEntities":260,"slug":18,"properties":261,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"98838621-06b4-4e11-93fd-fbf92261416f","2023-12-25T22:24:35.345+00:00",[],{"title":262},{"VI":263},"Department of Biochemistry and Immunology, National Institute of Veterinary Research, Hanoi, Vietnam",{"title":265},{"VI":266},"Anh Duc 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Zoonoses Project. 2012, 4: 1-119.\nAnonymous: The control of Neglected Zoonoses Diseases: A route to poverty alleviation. 2006, Geneva: WHO Press\nBlasco JM: A review of the use of B. melitensis Rev 1 vaccine in adult sheep and goats. Prev Vet Med. 1997, 31: 275-283. 10.1016\u002FS0167-5877(96)01110-5.\nMoriyón I, Grilló MJ, Monreal D, González D, Marín C, Lopez-Goñi I, Mainar-Jaime RC, Moreno E, Blasco JM: Rough vaccines in animal brucellosis: structural and genetic basis and present status. Vet Res. 2004, 35: 1-38. 10.1051\u002Fvetres:2003037.\nBarrio MB, Grilló MJ, Muñoz PM, Jacques I, González D, De-Miguel MJ, Marín CM, Barberan M, Letesson JJ, Gorvel JP, Moriyón I, Blasco JM, Zygmunt MS: Rough mutants defective in core and O-polysaccharide synthesis and export induce antibodies reacting in an indirect ELISA with smooth lipopolysaccharide and are less effective than Rev 1 vaccine against Brucella melitensis infection of sheep. Vaccine. 2009, 27: 1741-1749. 10.1016\u002Fj.vaccine.2009.01.025.\nGodfroid J, Scholz HC, Barbier T, Nicolas C, Wattiau P, Fretin D, Whatmore AM, Cloeckaert A, Blasco JM, Moriyón I, Saegerman C, Muma JB, Al-Dahouk S, Neubauer H, Letesson JJ: Brucellosis at the animal\u002Fecosystem\u002Fhuman interface at the beginning of the 21st century. Prev Vet Med. 2011, 102: 118-131. 10.1016\u002Fj.prevetmed.2011.04.007.\nMinas A, Minas M, Stournara A, Tselepidis S: The “effects” of Rev-1 vaccination of sheep and goats on human brucellosis in Greece. Prev Vet Med. 2004, 64: 41-47. 10.1016\u002Fj.prevetmed.2004.03.007.\nAlton GG, Jones LM, Angus RD, Verger JM: Techniques for the brucellosis laboratory. 1988, Paris, France: INRA\nGonzález D, Grilló MJ, De-Miguel MJ, Ali T, Arce-Gorvel V, Delrue RM, Conde-Álvarez R, Muñoz PM, Lopez-Goñi I, Iriarte M, Marín CM, Weintraub A, Widmalm G, Zygmunt M, Letesson JJ, Gorvel JP, Blasco JM, Moriyón I: Brucellosis vaccines: assessment of Brucella melitensis lipopolysaccharide rough mutants defective in core and O-polysaccharide synthesis and export. PLoS One. 2008, 3: e2760-10.1371\u002Fjournal.pone.0002760.\nMancilla M, Lopez-Goñi I, Moriyón I, Zarraga AM: Genomic Island 2 is an unstable genetic element contributing to Brucella lipopolysaccharide spontaneous smooth-to-rough dissociation. J Bacteriol. 2010, 192: 6346-6351. 10.1128\u002FJB.00838-10.\nVizcaíno N, Caro-Hernandez P, Cloeckaert A, Fernandez-Lago L: DNA polymorphism in the omp25\u002Fomp31 family of Brucella spp.: identification of a 1.7-kb inversion in Brucella cetaceae and of a 15.1-kb genomic island, absent from Brucella ovis, related to the synthesis of smooth lipopolysaccharide. Microbes Infect. 2004, 6: 821-834. 10.1016\u002Fj.micinf.2004.04.009.\nGarcía-Yoldi D, Marín CM, Lopez-Goñi I: Restriction site polymorphisms in the genes encoding new members of group 3 outer membrane protein family of Brucella spp. FEMS Microbiol Lett. 2005, 245: 79-84. 10.1016\u002Fj.femsle.2005.02.026.\nConde-Álvarez R, Arce-Gorvel V, Iriarte M, Mancek-Keber M, Barquero-Calvo E, Palacios-Chaves L, Chacón-Díaz C, Chaves-Olarte E, Martirosyan A, Von-Bargen K, Grilló MJ, Jerala R, Brandenburg K, Llobet E, Bengoechea JA, Moreno E, Moriyón I, Gorvel JP: The lipopolysaccharide core of Brucella abortus acts as a shield against innate immunity recognition. PLoS Pathog. 2012, 8: e1002675-10.1371\u002Fjournal.ppat.1002675.\nMancilla M, Marín CM, Blasco JM, Zarraga AM, Lopez-Goñi I, Moriyón I: Spontaneous excision of the O-polysaccharide wbkA glycosyltranferase gene is a cause of dissociation of smooth to rough Brucella colonies. J Bacteriol. 2012, 194: 1860-1867. 10.1128\u002FJB.06561-11.\nTurse JE, Pei J, Ficht TA: Lipopolysaccharide-deficient Brucella variants arise spontaneously during infection. Front Microbiol. 2011, 2: 54-\nVemulapalli R, McQuiston JR, Schurig GG, Sriranganathan N, Halling SM, Boyle SM: Identification of an IS711 element interrupting the wboA gene of Brucella abortus vaccine strain RB51 and a PCR assay to distinguish strain RB51 from other Brucella species and strains. Clin Diagn Lab Immunol. 1999, 6: 760-764.\nZygmunt MS, Blasco JM, Letesson JJ, Cloeckaert A, Moriyón I: DNA polymorphism analysis of Brucella lipopolysaccharide genes reveals marked differences in O-polysaccharide biosynthetic genes between smooth and rough Brucella species and novel species-specific markers. BMC Microbiol. 2009, 9: 92-10.1186\u002F1471-2180-9-92.\nDelVecchio VG, Kapatral V, Redkar RJ, Patra G, Mujer C, Los T, Ivanova N, Anderson I, Bhattacharyya A, Lykidis A, Reznik G, Jablonski L, Larsen N, D’Souza M, Bernal A, Mazur M, Goltsman E, Selkov E, Elzer PH, Hagius S, O’Callaghan D, Letesson JJ, Haselkorn R, Kyrpides N, Overbeek R: The genome sequence of the facultative intracellular pathogen Brucella melitensis. Proc Natl Acad Sci USA. 2002, 99: 443-448. 10.1073\u002Fpnas.221575398.\nNational Center for Biotechnology Information\u002FBasic Local Aligment Search Tool (NCBI\u002FBLAST). [http:\u002F\u002Fwww.ncbi.nlm.nih.gov\u002FBLAST]\nEuropean Molecular Biology Laboratory-European Bioinformatics Institute (EMBI-EBI). [http:\u002F\u002Fwww.ebi.ac.uk\u002FTools\u002Fclustalo]\nNational Center for Biotechnology Information\u002FPrimer-BLAST (NCBI\u002FPrimer-BLAST). [http:\u002F\u002Fwww.ncbi.nlm.nih.gov\u002Ftools\u002Fprimer-blast\u002F]\nWilson K: Preparation of genomic DNA from bacteria. Curr Protoc Mol Biol. 1997, 2.4.1-2.4.5.\nOcampo-Sosa AA, Aguero-Balbin J, Garcia-Lobo JM: Development of a new PCR assay to identify Brucella abortus biovars 5, 6 and 9 and the new subgroup 3b of biovar 3. Vet Microbiol. 2005, 110: 41-51. 10.1016\u002Fj.vetmic.2005.06.007.\nBosseray N: Brucella melitensis Rev.1 living attenuated vaccine: stability of markers, residual virulence and immunogenicity in mice. Biologicals. 1991, 19: 355-363. 10.1016\u002FS1045-1056(05)80025-9.\nGrilló MJ, Bosseray N, Blasco JM: In vitro markers and biological activity in mice of seed lot strains and commercial Brucella melitensis Rev 1 and Brucella abortus B19 vaccines. Biologicals. 2000, 28: 119-127. 10.1006\u002Fbiol.2000.0249.\nConde-Álvarez R, Grilló MJ, Salcedo SP, De-Miguel MJ, Fugier E, Gorvel JP, Moriyón I, Iriarte M: Synthesis of phosphatidylcholine, a typical eukaryotic phospholipid, is necessary for full virulence of the intracellular bacterial parasite Brucella abortus. Cell Microbiol. 2006, 8: 1322-1335. 10.1111\u002Fj.1462-5822.2006.00712.x.\nQuandt J, Hynes MF: Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria. Gene. 1993, 127: 15-21. 10.1016\u002F0378-1119(93)90611-6.\nSimon R, Priefer U, Pehle A: A broad host range mobilization system for the in vitro genetic engineering: transposon mutagenesis in gram negative bacteria. Biotechnology. 1983, 1: 784-890. 10.1038\u002Fnbt1183-784.\nRajashekara G, Covert J, Petersen E, Eskra L, Splitter G: Genomic island 2 of Brucella melitensis is a major virulence determinant: Functional analyses of genomic islands. J Bacteriol. 2008, 190: 6243-6252. 10.1128\u002FJB.00520-08.\nOy Growth Curves Ab Ltd. [http:\u002F\u002Fwww.bioscreen.fi]\nAragón V, Díaz R, Moreno E, Moriyón I: Characterization of Brucella abortus and Brucella melitensis native haptens as outer membrane O-type polysaccharides independent from the smooth lipopolysaccharide. J Bacteriol. 1996, 178: 1070-1079.\nGrilló MJ, Manterola L, De-Miguel MJ, Muñoz PM, Blasco JM, Moriyón I, Lopez-Goñi I: Increases of efficacy as vaccine against Brucella abortus infection in mice by simultaneous inoculation with avirulent smooth bvrS\u002FbvrR and rough wbkA mutants. Vaccine. 2006, 24: 2910-2916. 10.1016\u002Fj.vaccine.2005.12.038.\nOIE: Bovine Brucellosis. Manual of Diagnostic Tests and Vaccines for Terrestrial Animals. 2009, OIE, 1-35. Chapter 2.4.3\nGrilló MJ, Blasco JM, Gorvel JP, Moriyón I, Moreno E: What have we learned from brucellosis in the mouse model?. Vet Res. 2012, 43: 29-10.1186\u002F1297-9716-43-29.\nGerhardt P: The nutrition of Brucellae. Bacteriol Rev. 1958, 22: 91-98.\nCloeckaert A, Grayon M, Grepinet O: Identification of Brucella melitensis vaccine strain Rev.1 by PCR-RFLP based on a mutation in the rpsL gene. Vaccine. 2002, 20: 2546-2550. 10.1016\u002FS0264-410X(02)00159-7.\nMaisnier-Patin S, Berg OG, Liljas L, Andersson DI: Compensatory adaptation to the deleterious effect of antibiotic resistance in Salmonella Typhimurium. Mol Microbiol. 2002, 46: 355-366. 10.1046\u002Fj.1365-2958.2002.03173.x.\nManson JM, Gilmore MS: Pathogenicity island integrase cross-talk: a potential new tool for virulence modulation. Mol Microbiol. 2006, 61: 555-559. 10.1111\u002Fj.1365-2958.2006.05262.x.",{"EN":355},"Brucella melitensis Rev 1 is the best vaccine available for the prophylaxis of small ruminant brucellosis and, indirectly, for reducing human brucellosis. However, Rev 1 shows anomalously high rates of spontaneous dissociation from smooth (S) to rough (R) bacteria, the latter being inefficacious as vaccines. This S-R instability results from the loss of the O-polysaccharide. To overcome this problem, we investigated whether some recently described mechanisms promoting mutations in O-polysaccharide genes were involved in Rev 1 S-R dissociation. We found that a proportion of Rev 1 R mutants result from genome rearrangements affecting the wbo O-polysaccharide loci of genomic island GI-2 and the wbkA O-polysaccharide glycosyltransferase gene of the wbk region. Accordingly, we mutated the GI-2 int gene and the wbk IS transposase involved in those arrangements, and found that these Rev 1 mutants maintained the S phenotype and showed lower dissociation levels. Combining these two mutations resulted in a strain (Rev 2) displaying a 95% decrease in dissociation with respect to parental Rev 1 under conditions promoting dissociation. Rev 2 did not differ from Rev 1 in the characteristics used in Rev 1 typing (growth rate, colonial size, reactivity with O-polysaccharide antibodies, phage, dye and antibiotic susceptibility). Moreover, Rev 2 and Rev 1 showed similar attenuation and afforded similar protection in the mouse model of brucellosis vaccines. We conclude that mutations targeting genes and DNA sequences involved in spontaneous O-polysaccharide loss enhance the stability of a critical vaccine phenotype and complement the empirical stabilization precautions taken during S Brucella vaccine production.",{"EN":357},"Deletion of the GI-2 integrase and the wbkA flanking transposase improves the stability of Brucella melitensis Rev 1 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Methods 25:402–408",{"doi":831},"10.1006\u002Fmeth.2001.1262",{"id":18,"text":833,"url":18,"identifiers":834},"Iovine NM, Pursnani S, Voldman A, Wasserman G, Blaser MJ, Weinrauch Y (2008) Reactive nitrogen species contribute to innate host defense against Campylobacter jejuni. Infect Immun 76:986–993",{"doi":835},"10.1128\u002FIAI.01063-07",{"id":18,"text":837,"url":18,"identifiers":838},"R Development Core Team (2015) R: a language and environment for statistical computing. R Foundation for Statistical Computing, Vienna. ISBN 3-900051-07-0, http:\u002F\u002Fwww.R-project.org. Accessed 2016",{},{"id":18,"text":840,"url":18,"identifiers":841},"van Mourik A, Steeghs L, van Laar J, Meiring HD, Hamstra HJ, van Putten JP, Wosten MM (2010) Altered linkage of hydroxyacyl chains in lipid A of Campylobacter jejuni reduces TLR4 activation and antimicrobial resistance. J Biol Chem 285:15828–15836",{"doi":842},"10.1074\u002Fjbc.M110.102061",{"id":18,"text":844,"url":18,"identifiers":845},"Matsuguchi T, Musikacharoen T, Ogawa T, Yoshikai Y (2000) Gene expressions of Toll-like receptor 2, but not Toll-like receptor 4, is induced by LPS and inflammatory cytokines in mouse macrophages. J Immunol 165:5767–5772",{"doi":846},"10.4049\u002Fjimmunol.165.10.5767",{"id":18,"text":848,"url":18,"identifiers":849},"Nomura F, Akashi S, Sakao Y, Sato S, Kawai T, Matsumoto M, Nakanishi K, Kimoto M, Miyake K, Takeda K, Akira S (2000) Cutting edge: endotoxin tolerance in mouse peritoneal macrophages correlates with down-regulation of surface toll-like receptor 4 expression. J Immunol 164:3476–3479",{"doi":850},"10.4049\u002Fjimmunol.164.7.3476",{"id":18,"text":852,"url":18,"identifiers":853},"Pull SL, Doherty JM, Mills JC, Gordon JI, Stappenbeck TS (2005) Activated macrophages are an adaptive element of the colonic epithelial progenitor niche necessary for regenerative responses to injury. Proc Natl Acad Sci U S A 102:99–104",{"doi":854},"10.1073\u002Fpnas.0405979102",{"id":18,"text":856,"url":18,"identifiers":857},"Brown SL, Riehl TE, Walker MR, Geske MJ, Doherty JM, Stenson WF, Stappenbeck TS (2007) Myd88-dependent positioning of Ptgs2-expressing stromal cells maintains colonic epithelial proliferation during injury. J Clin Investig 117:258–269",{"doi":858},"10.1172\u002FJCI29159",{"id":18,"text":860,"url":18,"identifiers":861},"Hyun J, Romero L, Riveron R, Flores C, Kanagavelu S, Chung KD, Alonso A, Sotolongo J, Ruiz J, Manukyan A, Chun S, Singh G, Salas P, Targan SR, Fukata M (2015) Human intestinal epithelial cells express interleukin-10 through Toll-like receptor 4-mediated epithelial-macrophage crosstalk. J Innate Immun 7:87–101",{"doi":862},"10.1159\u002F000365417",{"id":864,"createTime":865,"updateTime":866,"relativeEntities":867,"slug":868,"properties":869,"entityType":187,"verifyStatus":188,"verifyTime":866,"verifyNote":190,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":110,"primaryUrl":878,"fullTextUrl":18,"authors":879,"publicationType":308,"publisherRelationship":962,"citationCount":18,"citationInfo":18,"publishDate":995,"publishYear":670,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":344},"4b0369de-c96d-4ac5-afee-9315ffbaad86","2023-12-19T22:12:57.849+00:00","2025-02-17T23:55:37.066+00:00",[],"MicroRNA-expression-profiling-of-goat-peripheral-blood-mononuclear-cells-in-response-to-peste-des-petits-ruminants-virus-infection",{"references":870,"abstract":872,"title":874,"doi":876},{"VOID":871},"Banyard AC, Parida S, Batten C, Oura C, Kwiatek O, Libeau G (2010) Global distribution of peste des petits ruminants virus and prospects for improved diagnosis and control. J Gen Virol 91:2885–2897\nGibbs EP, Taylor WP, Lawman MJ, Bryant J (1979) Classification of peste des petits ruminants virus as the fourth member of the genus Morbillivirus. Intervirology 11:268–274\nKumar KS, Babu A, Sundarapandian G, Roy P, Thangavelu A, Kumar KS, Arumugam R, Chandran ND, Muniraju M, Mahapatra M, Banyard AC, Manohar BM, Parida S (2014) Molecular characterisation of lineage IV peste des petits ruminants virus using multi gene sequence data. Vet Microbiol 174:39–49\nKumar N, Maherchandani S, Kashyap SK, Singh SV, Sharma S, Chaubey KK, Ly H (2014) Peste des petits ruminants virus infection of small ruminants: a comprehensive review. Viruses 6:2287–2327\nAlbina E, Kwiatek O, Minet C, Lancelot R, Servan de Almeida R, Libeau G (2013) Peste des petits ruminants, the next eradicated animal disease? Vet Microbiol 165:38–44\nDiallo A, Minet C, Le Goff C, Berhe G, Albina E, Libeau G, Barrett T (2007) The threat of peste des petits ruminants: progress in vaccine development for disease control. Vaccine 25:5591–5597\nSaravanan P, Sen A, Balamurugan V, Rajak KK, Bhanuprakash V, Palaniswami KS, Nachimuthu K, Thangavelu A, Dhinakarraj G, Hegde R, Singh RK (2010) Comparative efficacy of peste des petits ruminants (PPR) vaccines. Biologicals 38:479–485\nDiallo A, Barrett T, Barbron M, Subbarao SM, Taylor WP (1989) Differentiation of rinder pest and peste des petits ruminants viruses using specific cDNA clones. J Virol Methods 23:127–136\nPawar RM, Dhinakar Raj G, Balachandran C (2008) Relationship between thelevel of signaling lymphocyte activation molecule mRNA and replication of Peste-des-petits-ruminants virus in peripheral blood mononuclear cells of host animals. Acta Virol 52:231–236\nBolt G, Berg K, Blixenkrone-Moller M (2002) Measles virus-induced modulation of host-cell gene expression. J Gen Virol 83:1157–1165\nIwasa T, Suga S, Qi L, Komada Y (2010) Apoptosis of human peripheral blood mononuclear cells by wild-type measles virus infection is induced by interaction of hemagglutinin protein and cellular receptor, SLAM viacaspase-dependent pathway. Microbiol Immunol 54:405–416\nDhanasekaran S, Biswas M, Vignesh AR, Ramya R, Raj GD, Tirumurugaan KG, Raja A, Kataria RS, Parida S, Subbiah E (2014) Toll-like receptor responses to Peste des petits ruminants virus in goats and water buffalo. PLoS One 9:e111609\nManjunath S, Kumar GR, Mishra BP, Mishra B, Sahoo AP, Joshi CG, Tiwari AK, Rajak KK, Janga SC (2015) Genomic analysis of host–Peste des petits ruminants vaccine viral transcriptome uncovers transcription factors modulating immune regulatory pathways. Vet Res 46:15\nManjunath S, Mishra BP, Mishra B, Sahoo AP, Tiwari AK, Rajak KK, Muthuchelvan D, Saxena S, Santra L, Sahu AR, Wani SA, Singh RP, Singh YP, Pandey A, Kanchan S, Singh RK, Kumar GR, Janga SC (2017) Comparative and temporal transcriptome analysis of peste des petits ruminants virus infected goat peripheral blood mononuclear cells. Virus Res 229:28–40\nAxtell MJ, Westholm JO, Lai EC (2011) Vive la difference: biogenesis and evolution of microRNAs in plants and animals. Genome Biol 12:221\nBartel DP (2009) MicroRNAs: target recognition and regulatory functions. Cell 136:215–233\nShukla GC, Singh J, Barik S (2011) MicroRNAs: processing, maturation, target recognition and regulatory functions. Mol Cell Pharmacol 3:83–92\nHaasnoot J, Berkhout B (2011) RNAi and cellular miRNAs in infections bymammalian viruses. Methods Mol Biol 721:23–41\nSharma N, Singh SK (2016) Implications of non-coding RNAs in viral infections. 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Nature 451:1125–1129\nLiu G, Friggeri A, Yang Y, Park YJ, Tsuruta Y, Abraham E (2009) miR-147, a microRNA that is induced upon Toll-like receptor stimulation, regulates murine macrophage inflammatory responses. Proc Natl Acad Sci U S A 106:15819–15824\nPandey A, Sahu AR, Wani SA, Saxena S, Kanchan S, Sah V, Rajak KK, Khanduri A, Sahoo AP, Tiwari AK, Mishra B, Muthuchelvan D, Mishra BP, Singh RK, Gandham RK (2017) Modulation of host miRNAs transcriptome in lung and spleen of Peste des petits ruminants virus infected sheep and goats. Front Microbiol 8:1146\nWu J, Shen L, Chen J, Xu H, Mao L (2015) The role of microRNAs in enteroviral infections. Braz J Infect Dis 19:510–516\nChinnakannan SK, Nanda SK, Baron MD (2013) Morbillivirus v proteins exhibit multiple mechanisms to block type 1 and type 2 interferon signalling pathways. PLoS One 8:e57063\nMa X, Yang X, Nian X, Zhang Z, Dou Y, Zhang X, Luo X, Su J, Zhu Q, Cai X (2015) Identification of amino-acid residues in the V protein of peste des petits ruminants essential for interference and suppression of STAT-mediated interferon signaling. Virology 483:54–63\nSanz Bernardo B, Goodbourn S, Baron MD (2017) Control of the induction of type I interferon by Peste des petits ruminants virus. PLoS One 12:e0177300\nBaron J, Bin-Tarif A, Herbert R, Frost L, Taylor G, Baron MD (2014) Early changes in cytokine expression in peste des petits ruminants disease. Vet Res 45:22–33\nGao Z, Dou Y, Chen Y, Zheng Y (2014) MicroRNA roles in the NF- kappaB signaling pathway during viral infections. Biomed Res Int 2014:436097\nHoesel B, Schmid JA (2013) The complexity of NF-kappaB signaling in inflammation and cancer. Mol Cancer 12:86\nMondal B, Sreenivasa BP, Dhar P, Singh RP, Bandyopadhyay SK (2001) Apoptosis induced by peste des petits ruminants virus in goat peripheral blood mononuclear cells. Virus Res 73:113–119\nZhang Y, Wu S, Lv J, Feng C, Deng J, Wang C, Yuan X, Zhang T, Lin X (2013) Peste des petits ruminants virus exploits cellular autophagy machinery for replication. Virology 437:28–38",{"EN":873},"Peste des petits ruminants virus (PPRV) belongs to the genus Morbillivirus that causes an acute and highly contagious disease in goats and sheep. Virus infection can trigger the change in the cellular microRNA (miRNA) expression profile, which play important post-transcriptional regulatory roles in gene expression and can greatly influence viral replication and pathogenesis. Here, we employed deep sequencing technology to determine cellular miRNA expression profile in goat peripheral blood mononuclear cells (PBMC) infected with Nigeria 75\u002F1 vaccine virus, a widely used vaccine strain for mass vaccination programs against Peste des petits ruminants. Expression analysis demonstrated that PPRV infection can elicit 316 significantly differentially expressed (DE) miRNA including 103 known and 213 novel miRNA candidates in infected PBMC at 24 hours post-infection (hpi) as compared with a mock control. Target prediction and functional analysis of these DEmiRNA revealed significant enrichment for several signaling pathways including TLR signaling pathways, PI3K-Akt, endocytosis, viral carcinogenesis, and JAK-STAT signaling pathways. This study provides a valuable basis for further investigation of the roles of miRNA in PPRV replication and pathogenesis.",{"EN":875},"MicroRNA expression profiling of goat peripheral blood mononuclear cells in response to peste des petits ruminants virus infection",{"VOID":877},"10.1186\u002Fs13567-018-0565-3","https:\u002F\u002Fveterinaryresearch.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13567-018-0565-3",[880,897,914,926,938,950],{"id":881,"sortIndex":110,"researcher":18,"roles":882,"affiliations":883,"properties":894},"a2f26f68-17a2-4eb1-8e86-4663a5d1495b",[196],[884],{"id":18,"sortIndex":19,"affiliation":885,"properties":18},{"id":886,"createTime":887,"updateTime":888,"relativeEntities":889,"slug":890,"properties":891,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"5250e204-a7c2-4988-959b-69c95f15337c","2023-12-28T12:23:32.565+00:00","2025-01-30T23:11:01.701+00:00",[],"China-Institute-of-Veterinary-Drug-Control-Beijing-China",{"title":892},{"VI":893},"China Institute of Veterinary Drug Control, Beijing, China",{"title":895},{"VI":896},"Qinghong Xue",{"id":898,"sortIndex":112,"researcher":18,"roles":899,"affiliations":900,"properties":911},"85142074-b20a-4b68-966e-3ac818d8ff0a",[196],[901],{"id":18,"sortIndex":19,"affiliation":902,"properties":18},{"id":903,"createTime":904,"updateTime":905,"relativeEntities":906,"slug":907,"properties":908,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"97827e80-ee0e-4786-843f-5d3a957a30aa","2023-12-13T00:56:13.175+00:00","2024-09-12T23:20:51.068+00:00",[],"College-of-Veterinary-Medicine-Northwest-A-F-University-Yangling-China",{"title":909},{"VI":910},"College of Veterinary Medicine, Northwest A&F University, Yangling, China",{"title":912},{"VI":913},"Bo 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Nat Commun 11:5909\nSun Y, Liu J (2015) H9N2 influenza virus in China: a cause of concern. Protein Cell 6:18–25\nGuo Y, Dong J, Wang M, Zhang Y, Guo J, Wu K (2001) Characterization of hemagglutinin gene of influenza a virus subtype H9N2. Chin Med J 114:76–79\nGuo Y, Li J, Cheng X (1999) Discovery of men infected by avian influenza A (H9N2) virus. Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi 13:105–108\nButt KM, Smith GJ, Chen H, Zhang LJ, Leung YH, Xu KM, Lim W, Webster RG, Yuen KY, Peiris JS, Guan Y (2005) Human infection with an avian H9N2 influenza a virus in Hong Kong in 2003. J Clin Microbiol 43:5760–5767\nLiu R, Zhao B, Li Y, Zhang X, Chen S, Chen T (2018) Clinical and epidemiological characteristics of a young child infected with avian influenza A (H9N2) virus in China. J Int Med Res 46:3462–3467\nYuan R, Liang L, Wu J, Kang Y, Song Y, Zou L, Zhang X, Ni H, Ke C (2017) Human infection with an avian influenza A\u002FH9N2 virus in Guangdong in 2016. J Infect 74:422–425\nGuo YJ, Krauss S, Senne DA, Mo IP, Lo KS, Xiong XP, Norwood M, Shortridge KF, Webster RG, Guan Y (2000) Characterization of the pathogenicity of members of the newly established H9N2 influenza virus lineages in Asia. Virology 267:279–288\nLi CJ, Yu KZ, Tian GB, Yu DD, Liu LL, Jing B, Ping JH, Chen HL (2005) Evolution of H9N2 influenza viruses from domestic poultry in Mainland China. Virology 340:70–83\nBi J, Deng G, Dong J, Kong F, Li X, Xu Q, Zhang M, Zhao L, Qiao J (2010) Phylogenetic and molecular characterization of H9N2 influenza isolates from chickens in Northern China from 2007–2009. PLoS One 5:e13063\nDeng G, Bi J, Kong F, Li X, Xu Q, Dong J, Zhang M, Zhao L, Luan Z, Lv N, Qiao J (2010) Acute respiratory distress syndrome induced by H9N2 virus in mice. Arch Virol 155:187–195\nGuan Y, Shortridge KF, Krauss S, Webster RG (1999) Molecular characterization of H9N2 influenza viruses: were they the donors of the internal genes of H5N1 viruses in Hong Kong? Proc Natl Acad Sci USA 96:9363–9367\nYang L, Zhu W, Li X, Bo H, Zhang Y, Zou S, Gao R, Dong J, Zhao X, Chen W, Dong L, Zou X, Xing Y, Wang D, Shu Y (2017) Genesis and dissemination of highly pathogenic H5N6 avian influenza viruses. J Virol 91:e02116–e02199\nWu A, Su C, Wang D, Peng Y, Liu M, Hua S, Li T, Gao GF, Tang H, Chen J, Liu X, Shu Y, Peng D, Jiang T (2013) Sequential reassortments underlie diverse influenza H7N9 genotypes in China. Cell Host Microbe 14:446–452\nLiu D, Shi W, Gao GF (2014) Poultry carrying H9N2 act as incubators for novel human avian influenza viruses. Lancet 383:869\nGuo Y, Ding P, Li Y, Zhang Y, Zheng Y, Yu M, Suzuki Y, Zhang H, Ping J (2022) Genetic and biological properties of H10N3 avian influenza viruses: a potential pandemic candidate? Transbound Emerg Dis 69:e3171–e3182\nMehle A, Doudna JA (2008) An inhibitory activity in human cells restricts the function of an avian-like influenza virus polymerase. Cell Host Microbe 4:111–122\nManz B, Schwemmle M, Brunotte L (2013) Adaptation of avian influenza a virus polymerase in mammals to overcome the host species barrier. J Virol 87:7200–7209\nArunachalam R (2014) Adaptive evolution of a novel avian-origin influenza A\u002FH7N9 virus. Genomics 104:545–553\nLim K, Kim M, Lee MK, Ko J, Hong S, Choi BS (2014) Biophysical characterization of sites of host adaptive mutation in the influenza a virus RNA polymerase PB2 RNA-binding domain. Int J of Biochem and Cell B 53:237–245\nYu Z, Sun W, Li X, Chen Q, Chai H, Gao X, Guo J, Zhang K, Wang T, Feng N, Zheng X, Wang H, Zhao Y, Qin C, Huang G, Yang S, Hua Y, Zhang X, Gao Y, Xia X (2014) Adaptive amino acid substitutions enhance the virulence of a reassortant H7N1 avian influenza virus isolated from wild waterfowl in mice. Virology 476:233–239\nNeumann G, Watanabe T, Ito H, Watanabe S, Goto H, Gao P, Hughes M, Perez DR, Donis R, Hoffmann E, Hobom G, Kawaoka Y (1999) Generation of influenza a viruses entirely from cloned cDNAs. Proc Natl Acad Sci USA 96:9345–9350\nBrown EG (1990) Increased virulence of a mouse-adapted variant of influenza A\u002FFM\u002F1\u002F47 virus is controlled by mutations in genome segments 4, 5, 7, and 8. J Virol 64:4523–4533\nHoffmann E, Neumann G, Kawaoka Y, Hobom G, Webster RG (2000) A DNA transfection system for generation of influenza a virus from eight plasmids. Proc Natl Acad Sci USA 97:6108–6113\nBrown WM, Prager EM, Wang A, Wilson AC (1982) Mitochondrial DNA sequences of primates: tempo and mode of evolution. J Mol Evol 18:225–239\nSun X, Belser JA, Maines TR (2020) Adaptation of H9N2 influenza viruses to mammalian hosts: a review of molecular markers. Viruses 12:541\nLiu D, Shi W, Shi Y, Wang D, Xiao H, Li W, Bi Y, Wu Y, Li X, Yan J, Liu W, Zhao G, Yang W, Wang Y, Ma J, Shu Y, Lei F, Gao GF (2013) Origin and diversity of novel avian influenza a H7N9 viruses causing human infection: phylogenetic, structural, and coalescent analyses. Lancet 381:1926–1932\nMatrosovich MN, Krauss S, Webster RG (2001) H9N2 influenza a viruses from poultry in Asia have human virus-like receptor specificity. Virology 281:156–162\nLiang LB, Jiang L, Li JP, Zhao QQ, Wang JG, He XJ, Huang SY, Wang Q, Zhao YH, Wang GW, Sun N, Deng GH, Shi JZ, Tian GB, Zeng XY, Jiang YP, Liu LL, Liu JX, Chen PC, Bu ZG, Kawaoka Y, Chen HL, Li CJ (2019) Low polymerase activity attributed to PA drives the acquisition of the PB2 E627K mutation of H7N9 avian influenza virus in mammals. MBio 10:e01119–e01162\nChin AW, Li OT, Mok CK, Ng MK, Peiris M, Poon LL (2014) Influenza a viruses with different amino acid residues at PB2-627 display distinct replication properties in vitro and in vivo: revealing the sequence plasticity of PB2-627 position. Virology 468–470:545–555\nGabriel G, Dauber B, Wolff T, Planz O, Klenk HD, Stech J (2005) The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host. Proc Natl Acad Sci USA 102:18590–18595\nSong MS, Pascua PN, Lee JH, Baek YH, Lee OJ, Kim CJ, Kim H, Webby RJ, Webster RG, Choi YK (2009) The polymerase acidic protein gene of influenza a virus contributes to pathogenicity in a mouse model. J Virol 83:12325–12335\nBoulo S, Akarsu H, Ruigrok RW, Baudin F (2007) Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes. Virus Res 124:12–21\nYi C, Zhao Z, Wang S, Sun X, Zhang D, Sun X, Zhang A, Jin M (2017) Influenza A virus PA antagonizes interferon-β by interacting with interferon regulatory factor 3. Front Immunol 8:1051\nYuan P, Bartlam M, Lou Z, Chen S, Zhou J, He X, Lv Z, Ge R, Li X, Deng T, Fodor E, Rao Z, Liu Y (2009) Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site. Nature 458:909–913\nZhong G, Le MQ, Lopes TJS, Halfmann P, Hatta M, Fan S, Neumann G, Kawaoka Y (2018) Mutations in the PA protein of avian h5n1 influenza viruses affect polymerase activity and mouse virulence. J Virol 92:e01517–e01557\nBussey KA, Desmet EA, Mattiacio JL, Hamilton A, Bradel-Tretheway B, Bussey HE, Kim B, Dewhurst S, Takimoto T (2011) PA residues in the 2009 H1N1 pandemic influenza virus enhance avian influenza virus polymerase activity in mammalian cells. J Virol 85:7020–7028\nGarten RJ, Davis CT, Russell CA, Shu B, Lindstrom S, Balish A, Sessions WM, Xu X, Skepner E, Deyde V, Okomo-Adhiambo M, Gubareva L, Barnes J, Smith CB, Emery SL, Hillman MJ, Rivailler P, Smagala J, de Graaf M, Burke DF, Fouchier RA, Pappas C, Alpuche-Aranda CM, López-Gatell H, Olivera H, López I, Myers CA, Faix D, Blair PJ, Yu C et al (2009) Antigenic and genetic characteristics of swine-origin 2009 A(H1N1) influenza viruses circulating in humans. Science 325:197–201\nWu R, Zhang H, Yang K, Liang W, Xiong Z, Liu Z, Yang X, Shao H, Zheng X, Chen M, Xu D (2009) Multiple amino acid substitutions are involved in the adaptation of H9N2 avian influenza virus to mice. Vet Microbiol 138:85–91\nChan M, Leung A, Hisanaga T, Pickering B, Griffin BD, Vendramelli R, Tailor N, Wong G, Bi Y, Babiuk S, Berhane Y, Kobasa D (2020) H7N9 influenza virus containing a polybasic HA cleavage site requires minimal host adaptation to obtain a highly pathogenic disease phenotype in mice. 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Vet Microbiol 276:109615\nGao YW, Zhang Y, Shinya K, Deng GH, Jiang YP, Li ZJ, Guan YT, Tian GB, Li YB, Shi JZ, Liu LL, Zeng XY, Bu ZG, Xia XZ, Kawaoka Y, Chen HL (2009) Identification of amino acids in HA and PB2 critical for the transmission of H5N1 avian influenza viruses in a mammalian host. PLoS Pathog 5:e1000709\nLi X, Shi J, Guo J, Deng G, Zhang Q, Wang J, He X, Wang K, Chen J, Li Y, Fan J, Kong H, Gu C, Guan Y, Suzuki Y, Kawaoka Y, Liu L, Jiang Y, Tian G, Bu Z, Chen H (2014) Genetics, receptor binding property, and transmissibility in mammals of naturally isolated H9N2 avian influenza viruses. PLoS Pathog 10:e1004508\nFan M, Liang B, Zhao Y, Zhang Y, Liu Q, Tian M, Zheng Y, Xia H, Suzuki Y, Chen H, Ping J (2021) Mutations of 127, 183 and 212 residues on the HA globular head affect the antigenicity, replication and pathogenicity of H9N2 avian influenza virus. Transbound Emerg Dis 69:e659–e670\nSalomon R, Franks J, Govorkova EA, Ilyushina NA, Yen H-L, Hulse-Post DJ, Humberd J, Trichet M, Rehg JE, Webby RJ, Webster RG, Hoffmann E (2006) The polymerase complex genes contribute to the high virulence of the human H5N1 influenza virus isolate A\u002FVietnam\u002F1203\u002F04. J Exp Med 203:689–697\nBrown EG, Liu H, Kit LC, Baird S, Nesrallah M (2001) Pattern of mutation in the genome of influenza a virus on adaptation to increased virulence in the mouse lung: identification of functional themes. Proc Natl Acad Sci USA 98:6883–6888\nXu G, Zhang X, Gao W, Wang C, Wang J, Sun H, Sun Y, Guo L, Zhang R, Chang KC, Liu J, Pu J (2016) Prevailing PA mutation K356R in avian influenza H9N2 virus increases mammalian replication and pathogenicity. J Virol 90:8105–8114\nKawakami E, Watanabe T, Fujii K, Goto H, Watanabe S, Noda T, Kawaoka Y (2011) Strand-specific real-time RT-PCR for distinguishing influenza vRNA, cRNA, and mRNA. J Virol Methods 173:1–6\nFan S, Hatta M, Kim JH, Halfmann P, Imai M, Macken CA, Le MQ, Nguyen T, Neumann G, Kawaoka Y (2014) Novel residues in avian influenza virus PB2 protein affect virulence in mammalian hosts. Nat Commun 5:5021\nArai Y, Kawashita N, Ibrahim MS, Elgendy EM, Daidoji T, Ono T, Takagi T, Nakaya T, Matsumoto K, Watanabe Y (2019) PB2 mutations arising during H9N2 influenza evolution in the Middle East confer enhanced replication and growth in mammals. PLoS Pathog 15:e1007919",{"EN":1253},"The occurrence of human infections caused by avian H9N2 influenza viruses has raised concerns regarding the potential for human epidemics and pandemics. The molecular basis of viral adaptation to a new host needs to be further studied. Here, the bases of nucleotides 627 and 701 of PB2 were changed according to the uncoverable purine-to-pyrimidine transversion to block the development of PB2 627K and 701N mutations during serial passaging in mice. The purpose of this experiment was to identify key adaptive mutations in polymerase and NP genes that were obscured by the widely known host range determinants PB2 627K and 701N. Mouse-adapted H9N2 variants were obtained via twelve serial lung-to-lung passages. Sequence analysis showed that the mouse-adapted viruses acquired several mutations within the seven gene segments (PB2, PB1, PA, NP, HA, NA, and NS). One variant isolate with the highest polymerase activity possessed three substitutions, PB2 S155N, PA S49Y and D347G, which contributed to the highly virulent and mouse-adaptative phenotype. Further studies demonstrated that these three mutations resulted in increased polymerase activity, viral transcription and replication in mammalian cells, severe interstitial pneumonia, excessive inflammatory cellular infiltration and increased growth rates in mice. Our results suggest that the substitution of these three amino acid mutations may be an alternative strategy for H9N2 avian influenza viruses to adapt to mammalian hosts. The continued surveillance of zoonotic H9N2 influenza viruses should also include these mammalian adaptation markers as part of our pandemic preparedness efforts.",{"EN":1255},"Exploring the alternative virulence determinants PB2 S155N and PA S49Y\u002FD347G that promote mammalian adaptation of the H9N2 avian influenza virus in mice",{"VOID":1257},"10.1186\u002Fs13567-023-01221-6","https:\u002F\u002Fveterinaryresearch.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13567-023-01221-6",[1260,1275,1287,1299,1311,1323,1335],{"id":1261,"sortIndex":113,"researcher":18,"roles":1262,"affiliations":1263,"properties":1272},"69d92618-6e99-4d9c-ac42-72c4194c5d17",[196],[1264],{"id":18,"sortIndex":19,"affiliation":1265,"properties":18},{"id":1266,"createTime":1267,"updateTime":1267,"relativeEntities":1268,"slug":18,"properties":1269,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"54a6b31b-9905-440b-80bb-1f767066e388","2024-01-26T23:49:13.222+00:00",[],{"title":1270},{"VI":1271},"MOE International Joint Collaborative Research Laboratory for Animal Health and Food Safety & Jiangsu Engineering Research Center of Animal Immunology, College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, China",{"title":1273},{"VI":1274},"Bing Liang",{"id":1276,"sortIndex":109,"researcher":18,"roles":1277,"affiliations":1278,"properties":1284},"ea697314-0541-48b0-ad7c-b798ab368092",[196],[1279],{"id":18,"sortIndex":19,"affiliation":1280,"properties":18},{"id":1266,"createTime":1267,"updateTime":1267,"relativeEntities":1281,"slug":18,"properties":1282,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1283},{"VI":1271},{"title":1285},{"VI":1286},"Xuebing Bai",{"id":1288,"sortIndex":19,"researcher":18,"roles":1289,"affiliations":1290,"properties":1296},"da414702-091d-4f77-b082-a2238d07dbd8",[196],[1291],{"id":18,"sortIndex":19,"affiliation":1292,"properties":18},{"id":1266,"createTime":1267,"updateTime":1267,"relativeEntities":1293,"slug":18,"properties":1294,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1295},{"VI":1271},{"title":1297},{"VI":1298},"Yanna Guo",{"id":1300,"sortIndex":112,"researcher":18,"roles":1301,"affiliations":1302,"properties":1308},"96b5aa45-6146-4afb-9ff3-eea8b4c189f3",[196],[1303],{"id":18,"sortIndex":19,"affiliation":1304,"properties":18},{"id":1266,"createTime":1267,"updateTime":1267,"relativeEntities":1305,"slug":18,"properties":1306,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1307},{"VI":1271},{"title":1309},{"VI":1310},"Yiqing Zheng",{"id":1312,"sortIndex":294,"researcher":18,"roles":1313,"affiliations":1314,"properties":1320},"49f0a9d5-a627-4839-86ba-27758cf46299",[196],[1315],{"id":18,"sortIndex":19,"affiliation":1316,"properties":18},{"id":1266,"createTime":1267,"updateTime":1267,"relativeEntities":1317,"slug":18,"properties":1318,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1319},{"VI":1271},{"title":1321},{"VI":1322},"Jihui Ping",{"id":1324,"sortIndex":110,"researcher":18,"roles":1325,"affiliations":1326,"properties":1332},"72f97673-4125-47e4-a8f5-7cd6dc8ddf05",[196],[1327],{"id":18,"sortIndex":19,"affiliation":1328,"properties":18},{"id":1266,"createTime":1267,"updateTime":1267,"relativeEntities":1329,"slug":18,"properties":1330,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1331},{"VI":1271},{"title":1333},{"VI":1334},"Zhiyuan Liu",{"id":1336,"sortIndex":111,"researcher":18,"roles":1337,"affiliations":1338,"properties":1349},"3467f6c5-2bda-4764-aaf2-7fbe7c468f5d",[196],[1339],{"id":18,"sortIndex":19,"affiliation":1340,"properties":18},{"id":1341,"createTime":1342,"updateTime":1343,"relativeEntities":1344,"slug":1345,"properties":1346,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"ab880790-fd58-44bc-9cf5-66bbc6fd2153","2024-04-16T20:42:13.174+00:00","2025-01-30T11:58:46.344+00:00",[],"Department-of-Biochemistry-Microbiology-and-Immunology-Faculty-of-Medicine-University-of-Ottawa-Ottawa-Canada",{"title":1347},{"EN":1348},"Department of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Canada",{"title":1350},{"VI":1351},"Samar Dankar",{"url":1258,"publisher":1353,"properties":1380},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1354,"slug":10,"properties":1355,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1358,"manageAffiliations":1359,"indexDatabases":1360,"url":18,"thumbnailPath":18,"statistic":1375,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"eissn":1356,"title":1357},{"VOID":13},{"EN":15},[],[],[1361,1368],{"id":54,"indexDatabase":1362,"url":67,"indexYears":68,"academicFieldIds":1367,"indexDatabaseRanking":71},{"id":56,"createTime":57,"updateTime":58,"relativeEntities":1363,"label":1364,"description":1365,"key":64,"publicationTags":1366,"standard":18},[],{"EN":61,"VI":61},{"EN":61,"VI":63},[66],[70],{"id":73,"indexDatabase":1369,"url":88,"indexYears":18,"academicFieldIds":1374,"indexDatabaseRanking":18},{"id":75,"createTime":76,"updateTime":77,"relativeEntities":1370,"label":1371,"description":1372,"key":84,"publicationTags":1373,"standard":18},[],{"EN":80,"VI":80},{"VI":82,"EN":83},[86,87],[90],{"impactFactor":19,"impactFactorByYear":1376,"i10Index":105,"i10IndexLast5Year":106,"totalPublication":107,"totalPublicationByYear":1377,"totalCitation":126,"totalCitationByYear":1378,"totalCitationPerPublication":149,"totalCitationPerPublicationByYear":1379,"hindexLast5Year":167,"hindex":167},{"2012":93,"2013":94,"2014":95,"2015":96,"2016":97,"2017":98,"2018":99,"2019":100,"2020":101,"2021":102,"2022":103,"2023":104},{"2000":109,"2002":110,"2003":111,"2004":112,"2005":109,"2006":109,"2007":110,"2009":110,"2010":113,"2011":114,"2012":115,"2013":116,"2014":117,"2015":118,"2016":119,"2017":120,"2018":121,"2019":122,"2020":117,"2021":123,"2022":124,"2023":120,"2024":125},{"2000":128,"2002":129,"2003":130,"2004":131,"2005":132,"2006":133,"2007":134,"2009":135,"2010":136,"2011":137,"2012":138,"2013":139,"2014":140,"2015":141,"2016":142,"2017":143,"2018":144,"2019":145,"2020":146,"2021":147,"2022":148},{"2000":128,"2002":145,"2003":151,"2004":152,"2005":132,"2006":133,"2007":153,"2009":154,"2010":155,"2011":156,"2012":157,"2013":158,"2014":159,"2015":160,"2016":161,"2017":162,"2018":163,"2019":164,"2020":165,"2021":166,"2022":99},{"volume":1381,"pages":1383},{"VOID":1382},"54",{"VOID":1384},"1-17","2023-10-19",2023,{"id":1388,"createTime":1389,"updateTime":1390,"relativeEntities":1391,"slug":1392,"properties":1393,"entityType":187,"verifyStatus":188,"verifyTime":1390,"verifyNote":190,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":1402,"fullTextUrl":18,"authors":1403,"publicationType":308,"publisherRelationship":1858,"citationCount":18,"citationInfo":18,"publishDate":1890,"publishYear":343,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":344},"787f0535-f5e0-48a6-8e37-fac3fcb280c1","2024-01-17T19:53:28.878+00:00","2024-12-23T23:49:11.885+00:00",[],"The-lipopolysaccharide-outer-core-transferase-genes-pcgD-and-hptE-contribute-differently-to-the-virulence-of-Pasteurella-multocida-in-ducks",{"references":1394,"abstract":1396,"title":1398,"doi":1400},{"VOID":1395},"Wilson BA, Ho M (2013) Pasteurella multocida: from zoonosis to cellular microbiology. Clin Microbiol Rev 26:631–655\nAbreu F, Rodriguez-Lucas C, Rodicio MR, Vela AI, Fernandez-Garayzabal JF, Leiva PS, Cuesta F, Cid D, Fernandez J (2018) Human Pasteurella multocida infection with likely zoonotic transmission from a pet dog, Spain. Emerg Infect Dis 24:1145–1146\nBlackall PJ, Pahoff JL, Marks D, Fegan N, Morrow CJ (1995) Characterisation of Pasteurella multocida isolated from fowl cholera outbreaks on turkey farms. Aust Vet J 72:135–138\nKardos G, Kiss I (2005) Molecular epidemiology investigation of outbreaks of fowl cholera in geographically related poultry flocks. J Clin Microbiol 43:2959–2961\nMohamed MA, Mohamed MW, Ahmed AI, Ibrahim AA, Ahmed MS (2012) Pasteurella multocida in backyard chickens in Upper Egypt: incidence with polymerase chain reaction analysis for capsule type, virulence in chicken embryos and antimicrobial resistance. Vet Ital 48:77–86\nHarper M, John M, Turni C, Edmunds M, St Michael F, Adler B, Blackall PJ, Cox AD, Boyce JD (2015) Development of a rapid multiplex PCR assay to genotype Pasteurella multocida strains by use of the lipopolysaccharide outer core biosynthesis locus. J Clin Microbiol 53:477–485\nWilkie IW, Harper M, Boyce JD, Adler B (2012) Pasteurella multocida: diseases and pathogenesis. Curr Top Microbiol 361:1–22\nHarper M, Boyce JD, Adler B (2012) The key surface components of Pasteurella multocida: capsule and lipopolysaccharide. Curr Top Microbiol 361:39–51\nPetruzzi B, Briggs RE, Tatum FM, Swords WE, De Castro C, Molinaro A, Inzana TJ (2017) Capsular polysaccharide interferes with biofilm formation by Pasteurella multocida serogroup A. Bio 8:e01843-17\nZhao X, Liu Q, Xiao K, Hu Y, Liu X, Li Y, Kong Q (2016) Identification of the crp gene in avian Pasteurella multocida and evaluation of the effects of crp deletion on its phenotype, virulence and immunogenicity. BMC Microbiol 16:125\nSteen JA, Steen JA, Harrison P, Seemann T, Wilkie I, Harper M, Adler B, Boyce JD (2010) Fis is essential for capsule production in Pasteurella multocida and regulates expression of other important virulence factors. PLoS Pathog 6:e1000750\nMegroz M, Kleifeld O, Wright A, Powell D, Harrison P, Adler B, Harper M, Boyce JD (2016) The RNA-binding chaperone Hfq is an important global regulator of gene expression in Pasteurella multocida and plays a crucial role in production of a number of virulence factors, including hyaluronic acid capsule. Infect Immun 84:1361–1370\nXiao K, Liu Q, Liu X, Hu Y, Zhao X, Kong Q (2015) Identification of the Avian Pasteurella multocida phoP gene and evaluation of the effects of phoP deletion on virulence and immunogenicity. Int J Mol Sci 17:12\nCohen J (2002) The immunopathogenesis of sepsis. Nature 420:885–891\nTan Y, Kagan JC (2014) A cross-disciplinary perspective on the innate immune responses to bacterial lipopolysaccharide. Mol cell 54:212–223\nPeriasamy S, Praveena PE, Singh N (2018) Effects of Pasteurella multocida lipopolysaccharides on bovine leukocytes. Microb Pathog 119:225–232\nHoradagoda NU, Hodgson JC, Moon GM, Wijewardana TG, Eckersall PD (2002) Development of a clinical syndrome resembling haemorrhagic septicaemia in the buffalo following intravenous inoculation of Pasteurella multocida serotype B:2 endotoxin and the role of tumour necrosis factor-alpha. Res Vet Sci 72:194–200\nHarper M, Boyce JD (2017) The myriad properties of Pasteurella multocida lipopolysaccharide. Toxins 9:254\nHarper M, Boyce JD, Cox AD, St Michael F, Wilkie IW, Blackall PJ, Adler B (2007) Pasteurella multocida expresses two lipopolysaccharide glycoforms simultaneously, but only a single form is required for virulence: identification of two acceptor-specific heptosyl I transferases. Infect Immun 75:3885–3893\nSt Michael F, Harper M, Parnas H, John M, Stupak J, Vinogradov E, Adler B, Boyce JD, Cox AD (2009) Structural and genetic basis for the serological differentiation of Pasteurella multocida Heddleston serotypes 2 and 5. J Bacteriol 191:6950–6959\nBoyce JD, Harper M, St Michael F, John M, Aubry A, Parnas H, Logan SM, Wilkie IW, Ford M, Cox AD, Adler B (2009) Identification of novel glycosyltransferases required for assembly of the Pasteurella multocida A:1 lipopolysaccharide and their involvement in virulence. Infect Immun 77:1532–1542\nHarper M, Cox A, St Michael F, Parnas H, Wilkie I, Blackall PJ, Adler B, Boyce JD (2007) Decoration of Pasteurella multocida lipopolysaccharide with phosphocholine is important for virulence. J Bacteriol 189:7384–7391\nHarper M, Wright A, St Michael F, Li J, Deveson Lucas D, Ford M, Adler B, Cox AD, Boyce JD (2017) Characterization of two novel lipopolysaccharide phosphoethanolamine transferases in Pasteurella multocida and their role in resistance to cathelicidin-2. Infect Immun 85:e00557-e617\nHarper M, Cox AD, St Michael F, Wilkie IW, Boyce JD, Adler B (2004) A heptosyltransferase mutant of Pasteurella multocida produces a truncated lipopolysaccharide structure and is attenuated in virulence. Infect Immun 72:3436–3443\nHarper M, Boyce JD, Wilkie IW, Adler B (2003) Signature-tagged mutagenesis of Pasteurella multocida identifies mutants displaying differential virulence characteristics in mice and chickens. Infect Immun 71:5440–5446\nEdwards RA, Keller LH, Schifferli DM (1998) Improved allelic exchange vectors and their use to analyze 987P fimbria gene expression. Gene 207:149–157\nBosse JT, Durham AL, Rycroft AN, Kroll JS, Langford PR (2009) New plasmid tools for genetic analysis of Actinobacillus pleuropneumoniae and other pasteurellaceae. Appl Environ Microbiol 75:6124–6131\nKittelberger R, Hilbink F (1993) Sensitive silver-staining detection of bacterial lipopolysaccharides in polyacrylamide gels. J Biochem Biophys Methods 26:81–86\nLoh B, Grant C, Hancock RE (1984) Use of the fluorescent probe 1-N-phenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa. Antimicrob Agents Chemother 26:546–551\nLuo HY, Liu MF, Wang MS, Zhao XX, Jia RY, Chen S, Sun KF, Yang Q, Wu Y, Chen XY, Biville F, Zou YF, Jing B, Cheng AC, Zhu DK (2018) A novel resistance gene, lnu(H), conferring resistance to lincosamides in Riemerella anatipestifer CH-2. Int J Antimicrob Agents 51:136–139\nScott PC, Markham JF, Whithear KG (1999) Safety and efficacy of two live Pasteurella multocida aro-A mutant vaccines in chickens. Avian Dis 43:83–88\nHarper M, John M, Edmunds M, Wright A, Ford M, Turni C, Blackall PJ, Cox A, Adler B, Boyce JD (2016) Protective efficacy afforded by live Pasteurella multocida vaccines in chickens is independent of lipopolysaccharide outer core structure. Vaccine 34:1696–1703\nChung JY, Wilkie I, Boyce JD, Townsend KM, Frost AJ, Ghoddusi M, Adler B (2001) Role of capsule in the pathogenesis of fowl cholera caused by Pasteurella multocida serogroup A. Infect Immun 69:2487–2492\nOkuda S, Sherman DJ, Silhavy TJ, Ruiz N, Kahne D (2016) Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model. Nat Rev Microbiol 14:337–345\nChang PC, Wang CJ, You CK, Kao MC (2011) Effects of a HP0859 (rfaD) knockout mutation on lipopolysaccharide structure of Helicobacter pylori 26695 and the bacterial adhesion on AGS cells. Biochem Biophys Res Commun 405:497–502\nDam S, Pages JM, Masi M (2018) Stress responses, outer membrane permeability control and antimicrobial resistance in Enterobacteriaceae. Microbiology 164:260–267\nvan der Heijden J, Reynolds LA, Deng W, Mills A, Scholz R, Imami K, Foster LJ, Duong F, Finlay BB (2016) Salmonella rapidly regulates membrane permeability to survive oxidative stress. mBio 7:e01238-16\nBojkovic J, Richie DL, Six DA, Rath CM, Sawyer WS, Hu Q, Dean CR (2015) Characterization of an Acinetobacter baumannii lptD deletion strain: permeability defects and response to inhibition of lipopolysaccharide and fatty acid biosynthesis. J Bacteriol 198:731–741\nPark BS, Song DH, Kim HM, Choi BS, Lee H, Lee JO (2009) The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 458:1191–1195\nConde-Alvarez R, Arce-Gorvel V, Iriarte M, Mancek-Keber M, Barquero-Calvo E, Palacios-Chaves L, Chacon-Diaz C, Chaves-Olarte E, Martirosyan A, von Bargen K, Grillo MJ, Jerala R, Brandenburg K, Llobet E, Bengoechea JA, Moreno E, Moriyon I, Gorvel JP (2012) The lipopolysaccharide core of Brucella abortus acts as a shield against innate immunity recognition. PLoS Pathog 8:e1002675\nSchroeder TH, Lee MM, Yacono PW, Cannon CL, Gerceker AA, Golan DE, Pier GB (2002) CFTR is a pattern recognition molecule that extracts Pseudomonas aeruginosa LPS from the outer membrane into epithelial cells and activates NF-kappa B translocation. Proc Natl Acad Sci USA 99:6907–6912\nWeiss G, Schaible UE (2015) Macrophage defense mechanisms against intracellular bacteria. Immunol Rev 264:182–203\nRubires X, Saigi F, Pique N, Climent N, Merino S, Alberti S, Tomas JM, Regue M (1997) A gene (wbbL) from Serratia marcescens N28b (O4) complements the rfb-50 mutation of Escherichia coli K-12 derivatives. J Bacteriol 179:7581–7586",{"EN":1397},"Fowl cholera caused by Pasteurella multocida exerts a massive economic burden on the poultry industry. Lipopolysaccharide (LPS) is essential for the growth of P. multocida genotype L1 strains in chickens and specific truncations to the full length LPS structure can attenuate bacterial virulence. Here we further dissected the roles of the outer core transferase genes pcgD and hptE in bacterial resistance to duck serum, outer membrane permeability and virulence in ducks. Two P. multocida mutants, ΔpcgD and ΔhptE, were constructed, and silver staining confirmed that they all produced truncated LPS profiles. Inactivation of pcgD or hptE did not affect bacterial susceptibility to duck serum and outer membrane permeability but resulted in attenuated virulence in ducks to some extent. After high-dose inoculation, ΔpcgD showed remarkably reduced colonization levels in the blood and spleen but not in the lung and liver and caused decreased injuries in the spleen and liver compared with the wild-type strain. In contrast, the ΔhptE loads declined only in the blood, and ΔhptE infection caused decreased splenic lesions but also induced severe hepatic lesions. Furthermore, compared with the wild-type strain, ΔpcgD was significantly attenuated upon oral or intramuscular challenge, whereas ΔhptE exhibited reduced virulence only upon oral infection. Therefore, the pcgD deletion caused greater virulence attenuation in ducks, indicating the critical role of pcgD in P. multocida infection establishment and survival.",{"EN":1399},"The lipopolysaccharide outer core transferase genes pcgD and hptE contribute differently to the virulence of Pasteurella multocida in 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AH, Kirk MD, Torgerson PR, Gibb HJ, Hald T, Lake RJ, Praet N, Bellinger DC, De Silva NR, Gargouri N (2015) World Health Organization global estimates and regional comparisons of the burden of foodborne disease in 2010. PLoS Med 12:e1001923\nThrelfall E, Wain J, Peters T, Lane C, De Pinna E, Little C, Wales A, Davies R (2014) Egg-borne infections of humans with Salmonella: not only an S. Enteritidis problem. World’s Poult Sci J 70:15–26\nMoffatt CR, Musto J, Pingault N, Combs B, Miller M, Stafford R, Gregory J, Polkinghorne BG, Kirk MD (2017) Recovery of Salmonella enterica from Australian layer and processing environments following outbreaks linked to eggs. Foodborne Pathog Dis 14:478–482\nMoffatt CR, Musto J, Pingault N, Miller M, Stafford R, Gregory J, Polkinghorne BG, Kirk MD (2016) Salmonella Typhimurium and outbreaks of egg-associated disease in Australia, 2001 to 2011. Foodborne Pathog Dis 13:379–385\nOzFoodNet Working Group (2012) Monitoring the incidence and causes of diseases potentially transmitted by food in Australia: annual report of the Ozfoodnet network. Commun Dis Intell 36:42\nLindstedt B-A, Heir E, Gjernes E, Kapperud G (2003) DNA fingerprinting of Salmonella enterica subsp. enterica serovar Typhimurium with emphasis on phage type DT104 based on variable number of tandem repeat loci. J Clin Microbiol 41:1469–1479\nLindstedt B-A, Vardund T, Aas L, Kapperud G (2004) Multiple-locus variable-number tandem-repeats analysis of Salmonella enterica subsp. enterica serovar Typhimurium using PCR multiplexing and multicolor capillary electrophoresis. J Microbiol Methods 59:163–172\nLarsson J, Torpdahl M, Petersen R, Sørensen G, Lindsted B, Nielsen E (2009) Development of a new nomenclature for Salmonella Typhimurium multilocus variable number of tandem repeats analysis (MLVA). Euro Surveill 14:19174\nDyet K, Turbitt E, Carter P (2011) Multiple-locus variable-number tandem-repeat analysis for discriminating within Salmonella enterica serovar Typhimurium definitive types and investigation of outbreaks. Epidemiol Infect 139:1050–1059\nBarua H, Lindblom IL, Bisgaard M, Christensen JP, Olsen RH, Christensen H (2013) In vitro and in vivo investigation on genomic stability of Salmonella enterica Typhimurium DT41 obtained from broiler breeders in Denmark. Vet Microbiol 166:607–616\nWuyts V, Mattheus W, de Bex GDL, Wildemauwe C, Roosens NH, Marchal K, De Keersmaecker SC, Bertrand S (2013) MLVA as a tool for public health surveillance of human Salmonella Typhimurium: prospective study in Belgium and evaluation of MLVA loci stability. PLoS One 8:e84055\nDimovski K, Cao H, Wijburg OL, Strugnell RA, Mantena RK, Whipp M, Hogg G, Holt KE (2014) Analysis of Salmonella enterica serovar Typhimurium variable-number tandem-repeat data for public health investigation based on measured mutation rates and whole-genome sequence comparisons. J Bacteriol 196:3036–3044\nOctavia S, Wang Q, Tanaka MM, Sintchenko V, Lan R (2015) Genomic variability of serial human isolates of Salmonella enterica serovar Typhimurium associated with prolonged carriage. J Clin Microbiol 53:3507–3514\nMcWhorter AR, Chousalkar K (2018) A long-term efficacy trial of a live, attenuated Salmonella Typhimurium vaccine in layer hens. Front Microbiol 9:1380\nGast RK, Guard-Petter J, Holt PS (2003) Effect of prior serial in vivo passage on the frequency of Salmonella Enteritidis contamination in eggs from experimentally infected laying hens. Avian Dis 47:633–639\nOctavia S, Wang Q, Tanaka MM, Kaur S, Sintchenko V, Lan R (2015) Delineating community outbreaks of Salmonella enterica serovar Typhimurium by use of whole-genome sequencing: insights into genomic variability within an outbreak. J Clin Microbiol 53:1063–1071\nGole VC, Caraguel CG, Sexton M, Fowler C, Chousalkar KK (2014) Shedding of Salmonella in single age caged commercial layer flock at an early stage of lay. Int J Food Microbiol 189:61–66\nAkiba M, Kusumoto M, Iwata T (2011) Rapid identification of Salmonella enterica serovars, typhimurium, choleraesuis, infantis, hadar, enteritidis, dublin and gallinarum, by multiplex PCR. J Microbiol Methods 85:9–15\nPande VV, Gole VC, McWhorter AR, Abraham S, Chousalkar KK (2015) Antimicrobial resistance of non-typhoidal Salmonella isolates from egg layer flocks and egg shells. Int J Food Microbiol 203:23–26\nMaynard C, Fairbrother JM, Bekal S, Sanschagrin F, Levesque RC, Brousseau R, Masson L, Lariviere S, Harel J (2003) Antimicrobial resistance genes in enterotoxigenic Escherichia coli O149: K91 isolates obtained over a 23-year period from pigs. Antimicrob Agents Chemother 47:3214–3221\nWick RR, Judd LM, Gorrie CL, Holt KE (2017) Unicycler: resolving bacterial genome assemblies from short and long sequencing reads. PLoS Comput Biol 13:e1005595\nBankevich A, Nurk S, Antipov D, Gurevich AA, Dvorkin M, Kulikov AS, Lesin VM, Nikolenko SI, Pham S, Prjibelski AD (2012) SPAdes: a new genome assembly algorithm and its applications to single-cell sequencing. J Comput Biol 19:455–477\nWalker BJ, Abeel T, Shea T, Priest M, Abouelliel A, Sakthikumar S, Cuomo CA, Zeng Q, Wortman J, Young SK (2014) Pilon: an integrated tool for comprehensive microbial variant detection and genome assembly improvement. PLoS One 9:e112963\nWick RR, Schultz MB, Zobel J, Holt KE (2015) Bandage: interactive visualization of de novo genome assemblies. Bioinformatics 31:3350–3352\nGillespie JJ, Wattam AR, Cammer SA, Gabbard JL, Shukla MP, Dalay O, Driscoll T, Hix D, Mane SP, Mao C (2011) PATRIC: the comprehensive bacterial bioinformatics resource with a focus on human pathogenic species. Infect Immun 79:4286–4298\nAltschul SF, Gish W, Miller W, Myers EW, Lipman DJ (1990) Basic local alignment search tool. J Mol Biol 215:403–410\nTearle R (2019) Analysis of Salmonella genomes. https:\u002F\u002Fgithub.com\u002Fricktearle\u002FSalmonella. Accessed 12 Aug 2019\nPande VV, Devon RL, Sharma P, McWhorter AR, Chousalkar KK (2016) Study of Salmonella Typhimurium infection in laying hens. Front Microbiol 7:203\nJensen AN, Nielsen LR, Baggesen DL (2013) Use of real-time PCR on faecal samples for detection of sub-clinical Salmonella infection in cattle did not improve the detection sensitivity compared to conventional bacteriology. Vet Microbiol 163:373–377\nWilson IG (1997) Inhibition and facilitation of nucleic acid amplification. Appl Environ Microbiol 63:3741–3751\nGuard J, Sanchez-Ingunza R, Shah DH, Rothrock MJ, Gast RK, Jones DR (2015) Recovery of Salmonella enterica serovar Enteritidis from hens initially infected with serovar Kentucky. Food Chem 189:86–92\nHoward AJ, Chousalkar KK, McWhorter AR (2018) In vitro and in vivo efficacy of a live attenuated Salmonella Typhimurium vaccine at preventing intestinal colonization in chicks. Zoonoses Public Health 65:736–741\nBetts M, Russell R (2003) Amino acid properties and consequences of substitutions. In: Barnes MR, Gray IC (eds) Bioinformatics for geneticists. Wiley, Chichester\nOsman D, Cavet JS (2011) Metal sensing in Salmonella: implications for pathogenesis. Adv Microb Physiol 58:175–232\nRowinska-Zyrek M, Zakrzewska-Czerwinska J, Zawilak-Pawlik A, Kozlowski H (2014) Ni2+ chemistry in pathogens–a possible target for eradication. Dalton Trans 43:8976–8989\nMastroeni P, Morgan FJE, McKinley TJ, Shawcroft E, Clare S, Maskell DJ, Grant AJ (2011) Enhanced virulence of Salmonella enterica serovar Typhimurium after passage through mice. Infect Immun 79:636–643\nMartins M, McCusker MP, McCabe EM, O’Leary D, Duffy G, Fanning S (2013) Evidence of metabolic switching and implications for food safety from the phenome(s) of Salmonella enterica serovar Typhimurium DT104 cultured at selected points across the pork production food chain. Appl Environ Microbiol 79:5437–5449\nMcWhorter A, Chousalkar K (2015) Comparative phenotypic and genotypic virulence of Salmonella strains isolated from Australian layer farms. Front Microbiol 6:12\nLaboratory ASR (2014) October to December 2014 Quarterly Report. Institute of Medical and Veterinary Sciences, Adelaide\nLaboratory ASR (2015) April to June 2015 Quarterly Report. Institute of Medical and Veterinary Sciences, Adelaide\nSotomayor C, Wang Q, Arnott A, Howard P, Hope K, Lan R, Sintchenko V (2018) Novel Salmonella enterica serovar Typhimurium genotype levels as herald of seasonal salmonellosis epidemics. Emerg Infect Dis 24:1079–1082",{"EN":1901},"Eggs and raw or undercooked egg-containing food items are frequently identified as the bacterial source during epidemiolocal investigation of Salmonella outbreaks. Multi-locus variable number of tandem repeats analysis (MLVA) is a widely used Salmonella typing method enabling the study of diversity within populations of the same serotype. In vivo passage, however, has been linked with changes in MLVA type and more broadly the Salmonella genome. We sought to investigate whether in vivo passage through layer hens had an effect on MLVA type as well as the bacterial genome and whether any mutations affected bacterial virulence. Layer hens were infected with either Salmonella Typhimurium DT9 (03-24-11-11-523) as part of a single infection or were co-infected with an equal amount of Salmonella Mbandaka. Salmonella shedding in both single and co-infected birds was variable over the course of the 16-week experiment. Salmonella Typhimurium and Salmonella Mbandaka were identified in feces of co-infected birds. Salmonella colonies isolated from fecal samples were subtyped using MLVA. A single change in SSTR-6 was observed in Salmonella Typhimurium strains isolated from co-infected birds. Isolates of Salmonella Typhimurium of both the parent (03-24-11-11-523) and modified (03-24-12-11-523) MLVA type were sequenced and compared with the genome of the parent strain. Sequence analysis revealed that in vivo passaging resulted in minor mutation events. Passaged isolates exhibited significantly higher invasiveness in cultured human intestinal epithelial cells than the parent strain. The microevolution observed in this study suggests that changes in MLVA may arise more commonly and may have clinical significance.",{"EN":1903},"In vivo passage of Salmonella Typhimurium results in minor mutations in the bacterial genome and increases in vitro invasiveness",{"VOID":1905},"10.1186\u002Fs13567-019-0688-1","https:\u002F\u002Fveterinaryresearch.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13567-019-0688-1",[1908,1934,1946,1958],{"id":1909,"sortIndex":109,"researcher":18,"roles":1910,"affiliations":1911,"properties":1931},"04f96a96-fe2b-4a23-9815-e815f3d7902e",[196],[1912,1923],{"id":1913,"sortIndex":109,"affiliation":1914,"properties":1922},"4bd5bab7-dce6-4476-86e2-9311d9441841",{"id":1915,"createTime":1916,"updateTime":1916,"relativeEntities":1917,"slug":1918,"properties":1919,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"200d1c15-03c3-4b99-b2d4-0ac5d4c0a25c","2024-04-14T00:33:31.405+00:00",[],"Davies-Research-Centre-School-of-Animal-and-Veterinary-Sciences-The-University-of-Adelaide-Roseworthy-Australia",{"title":1920},{"EN":1921},"Davies Research Centre, School of Animal and Veterinary Sciences, The University of Adelaide, Roseworthy, Australia",{},{"id":18,"sortIndex":19,"affiliation":1924,"properties":18},{"id":1925,"createTime":1926,"updateTime":1926,"relativeEntities":1927,"slug":18,"properties":1928,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"14623e6d-36bd-4d83-8579-82f9e4c4e701","2023-12-17T16:14:41.405+00:00",[],{"title":1929},{"VI":1930},"School of Animal and Veterinary Sciences, The University of Adelaide, Roseworthy, Australia",{"title":1932},{"VI":1933},"Rick Tearle",{"id":1935,"sortIndex":110,"researcher":18,"roles":1936,"affiliations":1937,"properties":1943},"6e3ee3c6-0428-41c0-85e4-986c0848fee7",[196],[1938],{"id":18,"sortIndex":19,"affiliation":1939,"properties":18},{"id":1925,"createTime":1926,"updateTime":1926,"relativeEntities":1940,"slug":18,"properties":1941,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1942},{"VI":1930},{"title":1944},{"VI":1945},"Talia S. Moyle",{"id":1947,"sortIndex":113,"researcher":18,"roles":1948,"affiliations":1949,"properties":1955},"8be5f980-3fe0-404e-acd5-bc3c7952f42b",[196],[1950],{"id":18,"sortIndex":19,"affiliation":1951,"properties":18},{"id":1925,"createTime":1926,"updateTime":1926,"relativeEntities":1952,"slug":18,"properties":1953,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1954},{"VI":1930},{"title":1956},{"VI":1957},"Kapil K. Chousalkar",{"id":1959,"sortIndex":19,"researcher":18,"roles":1960,"affiliations":1961,"properties":1967},"ede1988e-4011-42fe-b091-99b008adc06c",[196],[1962],{"id":18,"sortIndex":19,"affiliation":1963,"properties":18},{"id":1925,"createTime":1926,"updateTime":1926,"relativeEntities":1964,"slug":18,"properties":1965,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1966},{"VI":1930},{"title":1968},{"VI":1969},"Andrea R. McWhorter",{"url":1906,"publisher":1971,"properties":1998},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1972,"slug":10,"properties":1973,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1976,"manageAffiliations":1977,"indexDatabases":1978,"url":18,"thumbnailPath":18,"statistic":1993,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"eissn":1974,"title":1975},{"VOID":13},{"EN":15},[],[],[1979,1986],{"id":54,"indexDatabase":1980,"url":67,"indexYears":68,"academicFieldIds":1985,"indexDatabaseRanking":71},{"id":56,"createTime":57,"updateTime":58,"relativeEntities":1981,"label":1982,"description":1983,"key":64,"publicationTags":1984,"standard":18},[],{"EN":61,"VI":61},{"EN":61,"VI":63},[66],[70],{"id":73,"indexDatabase":1987,"url":88,"indexYears":18,"academicFieldIds":1992,"indexDatabaseRanking":18},{"id":75,"createTime":76,"updateTime":77,"relativeEntities":1988,"label":1989,"description":1990,"key":84,"publicationTags":1991,"standard":18},[],{"EN":80,"VI":80},{"VI":82,"EN":83},[86,87],[90],{"impactFactor":19,"impactFactorByYear":1994,"i10Index":105,"i10IndexLast5Year":106,"totalPublication":107,"totalPublicationByYear":1995,"totalCitation":126,"totalCitationByYear":1996,"totalCitationPerPublication":149,"totalCitationPerPublicationByYear":1997,"hindexLast5Year":167,"hindex":167},{"2012":93,"2013":94,"2014":95,"2015":96,"2016":97,"2017":98,"2018":99,"2019":100,"2020":101,"2021":102,"2022":103,"2023":104},{"2000":109,"2002":110,"2003":111,"2004":112,"2005":109,"2006":109,"2007":110,"2009":110,"2010":113,"2011":114,"2012":115,"2013":116,"2014":117,"2015":118,"2016":119,"2017":120,"2018":121,"2019":122,"2020":117,"2021":123,"2022":124,"2023":120,"2024":125},{"2000":128,"2002":129,"2003":130,"2004":131,"2005":132,"2006":133,"2007":134,"2009":135,"2010":136,"2011":137,"2012":138,"2013":139,"2014":140,"2015":141,"2016":142,"2017":143,"2018":144,"2019":145,"2020":146,"2021":147,"2022":148},{"2000":128,"2002":145,"2003":151,"2004":152,"2005":132,"2006":133,"2007":153,"2009":154,"2010":155,"2011":156,"2012":157,"2013":158,"2014":159,"2015":160,"2016":161,"2017":162,"2018":163,"2019":164,"2020":165,"2021":166,"2022":99},{"volume":1999,"pages":2001},{"VOID":2000},"50",{"VOID":994},"2019-09-24",2019,{"id":2005,"createTime":2006,"updateTime":2007,"relativeEntities":2008,"slug":2009,"properties":2010,"entityType":187,"verifyStatus":188,"verifyTime":2007,"verifyNote":190,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":2019,"fullTextUrl":18,"authors":2020,"publicationType":308,"publisherRelationship":2123,"citationCount":18,"citationInfo":18,"publishDate":2156,"publishYear":2157,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":344},"82f22384-5b40-4095-b07f-c25b568cf6ca","2024-02-14T14:47:02.120+00:00","2025-02-18T23:45:37.058+00:00",[],"RNA-Seq-analysis-of-European-sea-bass-Dicentrarchus-labrax-L-infected-with-nodavirus-reveals-powerful-modulation-of-the-stress-response",{"references":2011,"abstract":2013,"title":2015,"doi":2017},{"VOID":2012},"FAO (2005–2019) Cultured aquatic species information programme: Dicentrarchus labrax. FAO fisheries and aquaculture Department\nMunday BL, Kwang J, Moody N (2002) Betanodavirus infections of teleost fish: a review. J Fish Dis 25:127–142\nNishizawa T, Furuhashi M, Nagai T, Nakai T, Muroga K (1997) Genomic classification of fish nodaviruses by molecular phylogenetic analysis of the coat protein gene. Appl Environ Microbiol 63:1633–1636\nDoan QK, Vandeputte M, Chatain B, Morin T, Allal F (2017) Viral encephalopathy and retinopathy in aquaculture: a review. J Fish Dis 40:717–742\nLu MW, Ngou FH, Chao YM, Lai YS, Chen NY, Lee FY, Chiou PP (2012) Transcriptome characterization and gene expression of Epinephelus spp in endoplasmic reticulum stress-related pathway during betanodavirus infection in vitro. Genomics 13:651\nLiu P, Wang L, Kwang J, Yue GH, Wong SM (2016) Transcriptome analysis of genes responding to NNV infection in Asian seabass epithelial cells. Fish Shellfish Immunol 54:342–352\nChaves-Pozo E, Valero Y, Esteve-Codina A, Gómez-Garrido J, Dabad M, Alioto T, Meseguer J, Esteban MA, Cuesta A (2017) Innate cell-mediated cytotoxic activity of European sea bass leucocytes against nodavirus-infected cells: a functional and RNA-seq study. Sci Rep 7:15396\nChen W, Yi L, Feng S, Liu X, Asim M, Zhou Y, Lan J, Jiang S, Tu J, Lin L (2017) Transcriptomic profiles of striped snakehead fish cells (SSN-1) infected with red-spotted grouper nervous necrosis virus (RGNNV) with an emphasis on apoptosis pathway. Fish Shellfish Immunol 60:346–354\nChaves-Pozo E, Bandín I, Olveira JG, Esteve-Codina A, Gómez-Garrido J, Dabad M, Alioto T, Esteban MÁ, Cuesta A (2019) European sea bass brain DLB-1 cell line is susceptible to nodavirus: a transcriptomic study. Fish Shellfish Immunol 1:14–24\nKim JO, Kim JO, Kim WS, Oh MJ (2017) Characterization of the transcriptome and gene expression of brain tissue in Sevenband gouper (Hyporthodus septemfasciatus) in response to NNV infection. Genes 8:E31\nLabella AM, Garcia-Rosado E, Bandín I, Dopazo CP, Castro D, Alonso MC, Borrego JJ (2018) Transcriptomic profiles of Senegalese sole infected with nervous necrosis virus reassortants presenting different degree of virulence. Front Immunol 9:1626\nTso CH, Lu MW (2018) Transcriptome profiling analysis of grouper during nervous necrosis virus persistent infection. Fish Shellfish Immunol 76:224–232\nWang L, Tian Y, Cheng M, Li Z, Li S, Wu Y, Zhang J, Ma W, Li W, Pang Z, Zhai J (2019) Transcriptome comparative analysis of immune tissues from asymptomatic and diseased Epinephelus moara naturally infected with nervous necrosis virus. Fish Shellfish Immunol 93:99–107\nPoisa-Beiro L, Dios S, Montes A, Aranguren R, Figueras A, Novoa B (2008) Nodavirus increases the expression of Mx and inflammatory cytokines in fish brain. Mol Immunol 45:218–225\nPoisa-Beiro L, Dios S, Ahmed H, Vasta GR, Martínez-López A, Estepa A, Alonso-Gutiérrez J, Figueras A, Novoa B (2009) Nodavirus infection of sea bass (Dicentrarchus labrax) induces up-regulation of galectin-1 expression with potential anti-inflammatory activity. J Immunol 183:6600–6611\nSarropoulou E, Sepulcre P, Poisa-Beiro L, Mulero V, Meseguer J, Figueras A, Novoa B, Terzoglou V, Reinhardt R, Magoulas A, Kotoulas G (2009) Profiling of infection specific mRNA transcripts of the European seabass Dicentrarchus labrax. BMC Genomics 10:157\nScapigliati G, Buonocore F, Randelli E, Casani D, Meloni S, Zarletti G, Tiberi M, Pietretti D, Boschi I, Manchado M, Martin-Antonio B, Jimenez-Cantizano R, Bovo G, Borghesan F, Lorenzen N, Einer-Jensen K, Adams S, Thompson K, Alonso C, Bejar J, Cano I, Borrego JJ, Alvarez MC (2010) Cellular and molecular immune responses of the sea bass (Dicentrarchus labrax) experimentally infected with betanodavirus. Fish Shellfish Immunol 28:303\nChaves-Pozo E, Guardiola FA, Meseguer J, Esteban MA, Cuesta A (2012) Nodavirus infection induces a great innate cell-mediated cytotoxic activity in resistant, gilthead seabream, and susceptible, European sea bass, teleost fish. Fish Shellfish Immunol 33:1159–1166\nNovel P, Fernandez-Trujillo MA, Gallardo-Galvez JB, Cano I, Manchado M, Buonocore F, Randelli E, Scapigliati G, Alvarez MC, Bejar J (2013) Two Mx genes identified in European sea bass (Dicentrarchus labrax) respond differently to VNNV infection. Vet Immunol Immunopathol 153:240–248\nValero Y, Morcillo P, Meseguer J, Buonocore F, Esteban MA, Chaves-Pozo E, Cuesta A (2015) Characterization of the interferon pathway in the teleost fish gonad against the vertically transmitted nervous necrosis virus. J Gen Virol 96:2176–2187\nBuonocore F, Randelli E, Tranfa P, Scapigliati G (2012) A CD83-like molecule in sea bass (Dicentrarchus labrax): molecular characterization and modulation by viral and bacterial infection. Fish Shellfish Immunol 32:1179–1184\nBuonocore F, Stocchi V, Nunez-Ortiz N, Randelli E, Gerdol M, Pallavicini A, Facchiano A, Bernini C, Guerra L, Scapigliati G, Picchietti S (2017) Immunoglobulin T from sea bass (Dicentrarchus labrax L.): molecular characterization, tissue localization and expression after nodavirus infection. BMC Mol Biol 18:8\nTort L (2011) Stress and immune modulation in fish. Dev Comp Immunol 35:1366–1375\nBovo G, Nishizawa T, Maltese C, Borghesan F, Mutinelli F, Montesi F, De Mas S (1999) Viral encephalopathy and retinopathy of farmed marine fish species in Italy. Virus Res 63:143–146\nReed LJ, Müench H (1938) A simple method of estimating fifty per cent end-points. Am J Hyg 27:493–497\nPfaffl MW (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29:2002–2007\nKuo HC, Wang TY, Chen PP, Chen YM, Chuang HC, Chen TY (2011) Real-time quantitative PCR assay for monitoring of nervous necrosis virus infection in grouper aquaculture. J Clin Microbiol 49:1090–1096\nMorgan JD, Iwama GK (1996) Cortisol-induced changes in oxygen consumption and ionic regulation in coastal cutthroat trout (Oncorhynchus clarki clarki) parr. Fish Physiol Biochem 15:385–394\nDong XX, Wang Y, Qin ZH (2009) Molecular mechanisms of excitotoxicity and their relevance to pathogenesis of neurodegenerative diseases. Acta Pharmacol Sin 30:379–387\nMennerich D, Kelokumpu S, Kietzmann T (2019) Hypoxia and reactive oxygen species as modulators of endoplasmic reticulum and Golgy homeostasis. Antioxid Redox Signal 30:113–137\nForrester JV, McMenamin PG, Dando SJ (2018) CNS infection and immune privilege. Nat Rev Neurosci 19:655–671\nKhansari AR, Parra D, Reyes-López FE, Tort L (2017) Modulatory in vitro effect of stress hormones on the cytokine response of rainbow trout and gilthead sea bream head kidney stimulated with Vibrio anguillarum bacterin. Fish Shellfish Immunol 70:736–749\nBenhar I, London A, Schwartz M (2012) The privileged immunity of immune privileged organs: the case of the eye. Front Immunol 3:296\nDios S, Poisa-Beiro L, Figueras A, Novoa B (2007) Suppression subtraction hybridization (SSH) and macroarray techniques reveal differential gene expression profiles in brain of sea bream infected with nodavirus. Mol Immunol 44:2195–2204\nGorissen M, Flik G (2016) The endocrinology of the stress response in fish: an adaptation-physiological view. In: Schreck CB, Tort L, Farrell AP, Brauner CJ (eds) Biology of stress in fish-fish physiology, vol 35. Academic Press, London\nBarton BA, Iwama GK (1991) Physiological changes in fish from stress in aquaculture with emphasis on the response and effects of corticosteroids. Ann Rev Fish Dis 1:13–26\nHeisler LK, Pronchuk N, Nonogaki K, Zhou L, Raber J, Tung L, Yeo GS, O’Rahilly S, Colmers WF, Elmquist JK, Tecott LH (2007) Serotonin activates the hypothalamic-pituitary-adrenal axis via serotonin 2C receptor stimulation. J Neurosci 27:6956–6964\nLevy BH, Tasker JG (2012) Synaptic regulation of the hypothalamic–pituitary–adrenal axis and its modulation by glucocorticoids and stress. Front Cell Neurosci 6:24\nLiu X, Khansari A, Teles M, Martínez-Rodríguez G, Zhang Y, Mancera JM, Reyes-López FE, Tort L (2019) Brain and pituitary response to vaccination in gilthead seabream (Sparus aurata L.). Front Physiol 10:717\nSchreck CB, Tort L (2016) The concept of stress in fish. In: Schreck CB, Tort L, Farrell AP, Brauner CJ (eds) Biology of stress in fish-fish physiology, vol 35. Academic Press, London\nYada T, Nakanishi T (2002) Interaction between endocrine and immune systems in fish. Int Rev Cytol 220:35–92\nPijanowski L, Jurecka P, Irnazarow I, Kepka M, Szwejser E, Verburg-van Kemenade BML, Chadzinska M (2015) Activity of the hypothalamus-pituitary-interrenal axis (HPI axis) and immune response in carp lines with different susceptibility to disease. Fish Physiol Biochem 41:1261–1278\nGrove S, Johansen R, Reitan LJ, Press CM, Dannevig BH (2006) Quantitative investigation of antigen and immune response in nervous and lymphoid tissues of Atlantic halibut (Hippoglossus hippoglossus) challenged with nodavirus. Fish Shellfish Immunol 21:525–539\nLópez-Muñoz A, Sepulcre MP, García-Moreno D, Fuentes I, Béjar J, Manchado M, Álvarez MC, Meseguer J, Mulero V (2012) Viral nervous necrosis virus persistently replicates in the central nervous system of asymptomatic gilthead seabream and promotes a transient inflammatory response followed by the infiltration of IgM + B lymphocytes. Dev Comp Immunol 37:429–437\nPiazzon MC, Galindo-Villegas J, Pereiro P, Estensoro I, Calduch-Giner JA, Gómez-Casado E, Novoa B, Mulero V, Sitjà-Bobadilla A, Pérez-Sánchez J (2016) Differential modulation of IgT and IgM upon parasitic, bacterial, viral, and dietary challenges in a perciform fish. Front Immunol 7:637\nParra D, Reyes-Lopez FE, Tort L (2015) Mucosal immunity and B cells in teleosts: effect of vaccination and stress. Front Immunol 6:354\nYada T, Nagae M, Moriyama S, Azuma T (1999) Effects of prolactin and growth hormone on plasma immunoglobulin M levels of hypophysectomized rainbow trout, Oncorhynchus mykiss. Gen Comp Endocrinol 115:46–52\nChen NC, Yoshimura M, Guan HH, Wang TY, Misumi Y, Lin CC, Chuankhayan P, Nakagawa A, Chan SI, Tsukihara T, Chen TY, Chen CJ (2015) Crystal structures of a piscine betanodavirus: mechanisms of capsid assembly and viral infection. PLoS Pathog 11:e1005203\nJang S, Oh D, Lee Y, Hosy E, Shin H, van Riesen C, Whitcomb D, Warburton JM, Jo J, Kim D, Kim SG, Um SM, Kwon SK, Kim MH, Roh JD, Woo J, Jun H, Lee D, Mah W, Kim H, Kaang BK, Cho K, Rhee JS, Choquet D, Kim E (2016) Synaptic adhesion molecule IgSF11 regulates synaptic transmission and plasticity. Nat Neurosci 19:84–93\nChen J, Kaul S, Simons SS Jr (2002) Structure\u002Factivity elements of the multifunctional protein, GMEB-1. Characterization of domains relevant for the modulation of glucocorticoid receptor transactivation properties. J Biol Chem 277:22053–22062\nPlotsky PM, Otto S, Sutton S (1987) Neurotransmitter modulation of corticotropin releasing factor secretion into the hypophysial-portal circulation. Life Sci 41:1311–1317\nSchulz JB, Matthews RT, Jenkins BG, Ferrante RJ, Siwek D, Henshaw DR, Cipolloni PB, Mecocci P, Kowall NW, Rosen BR (1995) Blockade of neuronal nitric oxide synthase protects against excitotoxicity in vivo. J Neurosci 15:8419–8429\nSchonbrunn A, Koch BD (1987) Mechanisms by which somatostatin inhibits pituitary hormone release. In: Reichlin S (ed) somatostatin. Springer, Boston\nCostanza M, Binart N, Steinman L, Pedotti R (2015) Prolactin: a versatile regulator of inflammation and autoimmune pathology. Autoimmun Rev 14:223–230\nRivero-Segura NA, Flores-Soto E, García de la Cadena S, Coronado-Mares I, Gomez-Verjan JC, Ferreira DG, Cabrera-Reyes EA, Lopes LV, Massieu L, Cerbón M (2017) Prolactin-induced neuroprotection against glutamate excitotoxicity is mediated by the reduction of [Ca2 +]i overload and NF-κB activation. PLoS One 12:e0176910\nGonzalez C, Corbacho AM, Eiserich JP, Garcia C, Lopez-Barrera F, Morales-Tlalpan V, Barajas-Espinosa A, Diaz-Muñoz M, Rubio R, Lin SH, Martinez de la Escalera G, Clapp C (2004) 16K-Prolactin inhibits activation of endothelial nitric oxide synthase, intracellular calcium mobilization, and endothelium-dependent vasorelaxation. Endocrinology 145:5714–5722\nWebster JI, Sternberg EM (2004) Role of the hypothalamic-pituitary-adrenal axis, glucocorticoids and glucocorticoid receptors in toxic sequelae of exposure to bacterial and viral products. J Endocrinol 181:207–221\nSilverman MN, Pearce BD, Biron CA, Miller AH (2005) Immune modulation of the hypothalamic-pituitary-adrenal (HPA) axis during viral infection. Viral Immunol 18:41–78\nCastric J, Thiéry R, Jeffroy J, de Kinkelin P, Raymond J (2001) Sea bream Sparus aurata, an asymptomatic contagious fish host for nodavirus. Dis Aquat Organ 47:33–38",{"EN":2014},"Nodavirus, or nervous necrosis virus (NNV), is the causative agent of viral encephalopathy and retinopathy (VER), a severe disease affecting numerous fish species worldwide. European sea bass, a cultured species of great economic importance, is highly susceptible to the disease. To better understand the response of this organism to NNV, we conducted RNA-Seq analysis of the brain and head kidney from experimentally infected and uninfected sea bass juveniles at 24 and 72 hours post-infection (hpi). Contrary to what was expected, we observed modest modulation of immune-related genes in the brain, the target organ of this virus, and some of these genes were even downregulated. However, genes involved in the stress response showed extremely high modulation. Accordingly, the genes encoding the enzymes implicated in the synthesis of cortisol were almost the only overexpressed genes in the head kidney at 24 hpi. This stress response was attenuated after 72 h in both tissues, and a progressive immune response against the virus was mounted. Moreover, experiments were conducted to determine how stress activation could impact NNV replication. Our results show the complex interplay between viral activity, the stress reaction and the immune response.",{"EN":2016},"RNA-Seq analysis of European sea bass (Dicentrarchus labrax L.) infected with nodavirus reveals powerful modulation of the stress response",{"VOID":2018},"10.1186\u002Fs13567-020-00784-y","https:\u002F\u002Fveterinaryresearch.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13567-020-00784-y",[2021,2048,2063,2075,2087,2099,2111],{"id":2022,"sortIndex":109,"researcher":18,"roles":2023,"affiliations":2024,"properties":2045},"964b742d-1e99-4e5f-97e0-a16dbbab1e3b",[196],[2025,2033],{"id":18,"sortIndex":19,"affiliation":2026,"properties":18},{"id":2027,"createTime":2028,"updateTime":2028,"relativeEntities":2029,"slug":18,"properties":2030,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"595c55e5-710e-4f9e-a960-df41e957e63f","2024-02-14T14:47:02.139+00:00",[],{"title":2031},{"VI":2032},"Institute of Marine Research (IIM), National Research Council (CSIC), Vigo, 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J Gen Virol 87:3451–3461. https:\u002F\u002Fdoi.org\u002F10.1099\u002Fvir.0.81999-0\nSigurdson CJ, Spraker TR, Miller MW, Oesch B, Hoover EA (2001) PrPCWD in the myenteric plexus, vagosympathetic trunk and endocrine glands of deer with chronic wasting disease. J Gen Virol 82:2327–2334. https:\u002F\u002Fdoi.org\u002F10.1099\u002F0022-1317-82-10-2327\nRace B, Meade-White KD, Miller MW, Barbian KD, Rubenstein R, LaFauci G, Cervenakova L, Favara C, Gardner D, Long D, Parnell M, Striebel J, Priola SA, Ward A, Williams ES, Race R, Chesebro B (2009) Susceptibilities of nonhuman primates to chronic wasting disease. Emerg Infect Dis 15:1366–1376. https:\u002F\u002Fdoi.org\u002F10.3201\u002Feid1509.090253\nMysterud A, Ytrehus B, Tranulis MA, Rauset GR, Rolandsen CM, Strand O (2020) Antler cannibalism in reindeer. 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J Wildl Manag 80:593–660. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fjwmg.1064\nWinter SN, Escobar LE (2020) Chronic wasting disease modeling: an overview. J Wildl Dis 56:741–758. https:\u002F\u002Fdoi.org\u002F10.7589\u002F2019-08-213\nMysterud A, Hopp P, Alvseike KR, Benestad SL, Nilsen EB, Rolandsen CM, Strand O, Våge J, Viljugrein H (2020) Hunting strategies to increase detection of chronic wasting disease in cervids. Nat Commun 11:4392. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41467-020-18229-7",{"EN":2168},"To date, chronic wasting disease (CWD) is the most infectious form of prion disease affecting several captive, free ranging and wild cervid species. Responsible for marked population declines in North America, its geographical spread is now becoming a major concern in Europe. Polymorphisms in the prion protein gene (PRNP) are an important factor influencing the susceptibility to prions and their rate of propagation. All reported cervid PRNP genotypes are affected by CWD. However, in each species, some polymorphisms are associated with lower attack rates and slower progression of the disease. This has potential consequences in terms of genetic selection, CWD diffusion and strain evolution. CWD also presents a zoonotic risk due to prions capacity to cross species barriers. This review summarizes our current understanding of CWD control, focusing on PRNP genetic, strain diversity and capacity to infect other animal species, including humans.",{"EN":2170},"Review on PRNP genetics and susceptibility to chronic wasting disease of Cervidae",{"VOID":2172},"10.1186\u002Fs13567-021-00993-z","https:\u002F\u002Fveterinaryresearch.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13567-021-00993-z",[2175,2190,2205,2220],{"id":2176,"sortIndex":109,"researcher":18,"roles":2177,"affiliations":2178,"properties":2187},"e975adfe-ff83-47a1-b52b-fde38eb7431b",[196],[2179],{"id":18,"sortIndex":19,"affiliation":2180,"properties":18},{"id":2181,"createTime":2182,"updateTime":2182,"relativeEntities":2183,"slug":18,"properties":2184,"entityType":38,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"9cd37eea-39b6-4dff-8bf4-66558c7200a2","2024-01-26T23:20:24.504+00:00",[],{"title":2185},{"VI":2186},"UMR INRAE ENVT 1225 - 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