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Methods in Molecular Biology PCR protocols: Current Methods and Applications. Edited by: Inc HP EUA. 1993, 81-87.\nYin JL, Shackel NA, Zekry A, McGuinness PH, Richards C, Putten KV, McCaughan GW, Eris JM, Bishop GA: Real-time reverse transcriptase-polymerase chain reaction (RT-PCR) for measurement of cytokine and growth factor mRNA expression with fluorogenic probes or SYBR Green I. Immunol Cell Biol. 2001, 79: 213-221. 10.1046\u002Fj.1440-1711.2001.01002.x.\nSchmitz M, Scheungraber C, Herrmann J, Teller K, Gajda M, Runnebaum IB, Durst M: Quantitative multiplex PCR assay for the detection of the seven clinically most relevant high-risk HPV types. J Clin Virol. 2009, 44: 302-307. 10.1016\u002Fj.jcv.2009.01.006.\nWatzinger F, Suda M, Preuner S, Baumgartinger R, Ebner K, Baskova L, Niesters HG, Lawitschka A, Lion T: Real-time quantitative PCR assays for detection and monitoring of pathogenic human viruses in immunosuppressed pediatric patients. J Clin Microbiol. 2004, 42: 5189-5198. 10.1128\u002FJCM.42.11.5189-5198.2004.\nCalonje E, Wilson Jones E: Tumors and Tumor-like conditions of blood vessels and lymphatics. Lever's Histopathology of the skin. Edited by: Elder D, Elenitsas R, Jaworsky C, Jhonson BJ. 1999, USA: Lippincott Williams & Wilkins, 623-651. 8\nMendez JC, Procop GW, Espy MJ, Paya CV, Smith TF: Detection and semiquantitative analysis of human herpesvirus 8 DNA in specimens from patients with Kaposi's sarcoma. J Clin Microbiol. 1998, 36: 2220-2222.\nKennedy MM, Cooper K, Howells DD, Picton S, Biddolph S, Lucas SB, McGee JO, O'Leary JJ: Identification of HHV8 in early Kaposi's sarcoma: implications for Kaposi's sarcoma pathogenesis. Mol Pathol. 1998, 51: 14-20. 10.1136\u002Fmp.51.1.14.\nCoombs NJ, Gough AC, Primrose JN: Optimisation of DNA and RNA extraction from archival formalin-fixed tissue. Nucleic Acids Res. 1999, 27: e12-10.1093\u002Fnar\u002F27.16.e12.\nPyakurel P, Pak F, Mwakigonja AR, Kaaya E, Biberfeld P: KSHV\u002FHHV-8 and HIV infection in Kaposi's sarcoma development. Infect Agent Cancer. 2007, 2: 4-10.1186\u002F1750-9378-2-4.\nZeng Y, Zhang X, Huang Z, Cheng L, Yao S, Qin D, Chen X, Tang Q, Lv Z, Zhang L, Lu C: Intracellular Tat of human immunodeficiency virus type 1 activates lytic cycle replication of Kaposi's sarcoma-associated herpesvirus: role of JAK\u002FSTAT signaling. J Virol. 2007, 81: 2401-2417. 10.1128\u002FJVI.02024-06.\nde Souza VA, Sumita LM, Nascimento MC, Oliveira J, Mascheretti M, Quiroga M, Freire WS, Tateno A, Boulos M, Mayaud P, Pannuti CS: Human herpesvirus-8 infection and oral shedding in amerindian and non-amerindian populations in the brazilian Amazon region. J Infect Dis. 2007, 196: 844-852. 10.1086\u002F520549.\nAl-Otaibi LM, Ngui SL, Scully CM, Porter SR, Teo CG: Salivary human herpesvirus 8 shedding in renal allograft recipients with Kaposi's sarcoma. J Med Virol. 2007, 79: 1357-1365. 10.1002\u002Fjmv.20929.\nLeao JC, Caterino-De-Araujo A, Porter SR, Scully C: Human herpesvirus 8 (HHV-8) and the etiopathogenesis of Kaposi's sarcoma. Rev Hosp Clin Fac Med Sao Paulo. 2002, 57: 175-186.\nKouri V, Eng SM, Rodriguez ME, Resik S, Orraca O, Moore PS, Chang Y: Seroprevalence of Kaposi's sarcoma-associated herpesvirus in various populations in Cuba. Rev Panam Salud Publica. 2004, 15: 320-325. 10.1590\u002FS1020-49892004000500006.\nGasperini P, Barbierato M, Martinelli C, Rigotti P, Marchini F, Masserizzi G, Leoncini F, Chieco-Bianchi L, Schulz TF, Calabro ML: Use of a BJAB-derived cell line for isolation of human herpesvirus 8. J Clin Microbiol. 2005, 43: 2866-2875. 10.1128\u002FJCM.43.6.2866-2875.2005.\nBoivin G, Cote S, Cloutier N, Abed Y, Maguigad M, Routy JP: Quantification of human herpesvirus 8 by real-time PCR in blood fractions of AIDS patients with Kaposi's sarcoma and multicentric Castleman's disease. J Med Virol. 2002, 68: 399-403. 10.1002\u002Fjmv.10217.\nMartro E, Cannon MJ, Dollard SC, Spira TJ, Laney AS, Ou CY, Pellett PE: Evidence for both lytic replication and tightly regulated human herpesvirus 8 latency in circulating mononuclear cells, with virus loads frequently below common thresholds of detection. J Virol. 2004, 78: 11707-11714. 10.1128\u002FJVI.78.21.11707-11714.2004.\nHarrington WJ, Bagasra O, Sosa CE, Bobroski LE, Baum M, Wen XL, Cabral L, Byrne GE, Pomerantz RJ, Wood C: Human herpesvirus type 8 DNA sequences in cell-free plasma and mononuclear cells of Kaposi's sarcoma patients. J Infect Dis. 1996, 174: 1101-1105.\nKuo CP, Wu CL, Ho HT, Chen CG, Liu SI, Lu YT: Detection of cytomegalovirus reactivation in cancer patients receiving chemotherapy. Clin Microbiol Infect. 2008, 14: 221-227. 10.1111\u002Fj.1469-0691.2007.01895.x.\nGarrigue I, Doussau A, Asselineau J, Bricout H, Couzi L, Rio C, Merville P, Fleury H, Lafon ME, Thiebaut R: Prediction of cytomegalovirus (CMV) plasma load from evaluation of CMV whole-blood load in samples from renal transplant recipients. J Clin Microbiol. 2008, 46: 493-498. 10.1128\u002FJCM.01499-07.\nBrantsaeter AB, Holberg-Petersen M, Jeansson S, Goplen AK, Bruun JN: CMV quantitative PCR in the diagnosis of CMV disease in patients with HIV-infection-a retrospective autopsy based study. BMC Infect Dis. 2007, 7: 127-10.1186\u002F1471-2334-7-127.\nPolstra AM, Cornelissen M, Goudsmit J, van der Kuyl AC: Retrospective, longitudinal analysis of serum human herpesvirus-8 viral DNA load in AIDS-related Kaposi's sarcoma patients before and after diagnosis. J Med Virol. 2004, 74: 390-396. 10.1002\u002Fjmv.20192.\nMoore PS, Chang Y: Kaposi's Sarcoma-Associated Herpesvirus. Fields Virology. Edited by: Knipe DM, Howley PM, Griffin DE, Lamb RAM MA, Roizman B, Straus SE. 2001, USA: LIPPINCOTT WILLIAMS & WILKINS, 2: 2803-2833. 4\nNawar E, Mbulaiteye SM, Gallant JE, Wohl DA, Ardini M, Hendershot T, Goedert JJ, Rabkin CS: Risk factors for Kaposi's sarcoma among HHV-8 seropositive homosexual men with AIDS. Int J Cancer. 2005, 115: 296-300. 10.1002\u002Fijc.20887.\nAlkharsah KR, Dedicoat M, Blasczyk R, Newton R, Schulz TF: Influence of HLA Alleles on Shedding of Kaposi Sarcoma-Associated Herpesvirus in Saliva in an African Population. J Infect Dis. 2007, 195: 809-816. 10.1086\u002F511827.\nCasper C, Carrell D, Miller KG, Judson FD, Meier AS, Pauk JS, Morrow RA, Corey L, Wald A, Celum C: HIV serodiscordant sex partners and the prevalence of human herpesvirus 8 infection among HIV negative men who have sex with men: baseline data from the EXPLORE Study. Sex Transm Infect. 2006, 82: 229-235. 10.1136\u002Fsti.2005.016568.\nCorbellino M, Pizzuto M, Bestetti G, Corsico L, Piazza M, Pigozzi B, Galli M, Baldini L, Neri A, Parravicini C: Absence of Kaposi's sarcoma--associated herpesvirus DNA sequences in multiple myeloma. Blood. 1999, 93: 1110-1111.\nViviano E, Gallo E, Bongiorno MR, Romano N: [The genomic sequences of the human herpesvirus 8 in biological samples from HIV-positive and-negative subjects in Sicily]. Ann Ig. 1999, 11: 507-509.\nEngels EA, Atkinson JO, Graubard BI, McQuillan GM, Gamache C, Mbisa G, Cohn S, Whitby D, Goedert JJ: Risk Factors for Human Herpesvirus 8 Infection among Adults in the United States and Evidence for Sexual Transmission. J Infect Dis. 2007, 196: 199-207. 10.1086\u002F518791.\nTaylor MM, Chohan B, Lavreys L, Hassan W, Huang ML, Corey L, Ashley Morrow R, Richardson BA, Mandaliya K, Ndinya-Achola J, et al: Shedding of human herpesvirus 8 in oral and genital secretions from HIV-1-seropositive and-seronegative Kenyan women. J Infect Dis. 2004, 190: 484-488. 10.1086\u002F421466.",{"EN":38},"In Cuba, previous reports have shown an increase of epidemic KS, reaching a total of 120 cases by the end of 2007, despite the use of HAART. To evaluate and compare the role of human herpes virus 8 (HHV-8) viral loads in different compartments of AIDS-related Kaposi's sarcoma (AIDS-KS) patients real-time polymerase chain reaction (RT-PCR) was used to determine the genome copy number of HHV-8 in plasma, saliva, tissue and peripheral blood mononuclear cells (PBMC) of 49 AIDS-KS patients. Overall, 98% of AIDS-KS patients harbored detectable HHV-8. HHV-8 could be detected in 91.6% of KS tissue lesions showing the highest viral load (median log = 3.14 copies\u002F100 ng DNA) followed by saliva and PBMC which were positive in 78%, and 69.2%; respectively. In contrast, HHV-8 was detected in only 37% of plasma samples, which also showed lower viral loads. Men who had sex with men (MSM) were more likely to have three-times higher HHV-8 genome copies in KS lesions when compared with tissues from heterosexuals individuals (OR 3; 95% CI 1.1 to 12.5). These results emphasize the systemic nature of HHV-8-infection and demonstrate the possible role of saliva in HHV-8 transmission among MSM.",{"EN":40},"Simultaneous quantification of human herpesvirus 8 DNA by real time PCR in different tissues of HIV infected cuban patients with Kaposi's sarcoma",{"VOID":42},"10.1186\u002F2042-4280-1-3","PUBLICATION","VERIFIED","Auto 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GJ: RNA interference. Nature. 2002, 418: 244-251. 10.1038\u002F418244a.\nNakayashiki H: HRNA silencing in fungi: mechanisms and applications. FEBS Lett. 2005, 579: 5950-5957. 10.1016\u002Fj.febslet.2005.08.016.\nGrishok A: RNAi mechanisms in Caenorhabditis elegans. FEBS Lett. 2005, 579: 5932-5939. 10.1016\u002Fj.febslet.2005.08.001.\nBartel DP: MicroRNAs: genomics, biogenesis, mechanism, and function. Cell. 2004, 116: 281-297. 10.1016\u002FS0092-8674(04)00045-5.\nJacque JM, Triques K, Stevenson M: Modulation of HIV-1 replication by RNA interference. Nature. 2002, 418: 435-438. 10.1038\u002Fnature00896.\nNovina CD, Murray MF, Dykxhoorn DM, Beresford PJ, Riess J, Lee SK, Collman RG, Lieberman J, Shankar P, Sharp PA: siRNA-directed inhibition of HIV-1 infection. Nat Med. 2002, 8: 681-686.\nBenasser Y, Le SY, Benkirane M, Jiang KT: Evidence that HIV-1 encodes a siRNA and a suppressor of RNA silencing. Immunity. 2005, 22: 607-619. 10.1016\u002Fj.immuni.2005.03.010.\nHamasaki K, Nakao K, Matsumoto K, Ichikawa T, Ishikawa H, Eguchi K: Short interfering RNA-directed inhibition of hepatitis B virus replication. FEBS Lett. 2003, 543: 51-54. 10.1016\u002FS0014-5793(03)00400-9.\nKapadia SB, Brideau-Andersen A, Chisari FV: Interference of hepatitis C virus RNA replication by short interfering RNAs. Proc Natl Acad Sci USA. 2003, 100: 2014-2018. 10.1073\u002Fpnas.252783999.\nKusov Y, Kanda T, Palmenberg A, Sgro JY, Gauss-Muller V: Silencing of hepatitis A virus infection by small interfering RNAs. J Virol. 2006, 80: 5599-5610. 10.1128\u002FJVI.01773-05.\nFranz AW, Sanchez-Vargas I, Adelman ZN, Blair CD, Beaty BJ, James AA, Olson KE: Engineering RNA interference-based resistance to dengue virus type 2 in genetically modified Aedes aegypti. Proc Natl Acad Sci USA. 2006, 103: 4198-4203. 10.1073\u002Fpnas.0600479103.\nGe Q, McManus MT, Nguyen T, Shen CH, Sharp PA, Eisen NH, Chen J: RNA interference of influenza virus production by directly targeting mRNA for degradation and indirectly inhibiting all viral RNA transcription. Proc Natl Acad Sci USA. 2003, 100: 2718-2723. 10.1073\u002Fpnas.0437841100.\nGitlin L, Stone JK, Andino R: Poliovirus escape from RNA interference: short interfering RNA-target recognition and implications for therapeutic approaches. J Virol. 2005, 79: 1027-1035. 10.1128\u002FJVI.79.2.1027-1035.2005.\nBhuyan PK, Karikò K, Capodici J, Lubinski J, Hook LM, Friedman HM, Weissman D: Short interfering RNA-mediated inhibition of herpes simplex virus type 1 gene expression and function during infection of human keratinocytes. 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Cell. 1998, 93: 705-716. 10.1016\u002FS0092-8674(00)81433-6.\nKavi HH, Xie W, Fernandez HR, Birchler JA: Global analysis of siRNA-mediated transcriptional gene silencing. Bioessays. 2005, 27: 1209-1212. 10.1002\u002Fbies.20328.\nPedersen AG, Nielsen H: Neural network prediction of translation initiation sites in eukaryotes: perspectives for EST and genome analysis. ISMB. 1997, 5: 226-233.\nPesole G, Mignone F, Gissi C, Grillo G, Licciulli F, Liuni F: Structural and functional features of eukaryotic untranslated regions. Gene. 2001, 276: 73-81. 10.1016\u002FS0378-1119(01)00674-6.\nMesserle M, Buhler B, Keil GM, Koszinowski UH: Structural organization, expression, and functional characterization of the murine cytomegalovirus immediate-early gene 3. J Virol. 1992, 66: 27-36.",{"EN":269},"Murine cytomegalovirus (MCMV) is closely related to human cytomegalovirus (HCMV) which is responsible for a variety of diseases, including retinitis, in immunocompromised individuals. Small inhibitory RNA molecules directed against essential viral regulatory genes may prove clinically useful. Small hairpin RNAs (shRNAs) directed against the essential MCMV immediate early-3 gene (IE-3) were designed and tested in vitro at m.o.i.'s of 2 and 0.2 to determine if virus replication could be inhibited. At m.o.i. = 2, a MCMV IE-3 specific shRNA specific for sequences at the beginning of exon 5 inhibited virus replication with a maximum decrease in virus titer of approximately two logs at day 5 p.i. Surprisingly, however, at m.o.i. = 0.2, the same shRNA enhanced virus replication. In the latter case, the main IE-3 product observed in infected cells was not the expected 88 kd full length IE-3 protein observed at high m.o.i. but rather a truncated 45 kd form of this protein. Rapid analysis of 5' cDNA ends (5' RACE) indicated that substantial differences exist in the transcript profile produced by the IE-3 gene at low and high m.o.i. early after infection and that multiple transcripts are produced under both conditions. One such transcript, which originated in exon 5 of the IE-3 gene, was located outside the region targeted by our shRNA and was the major transcript produced at low m.o.i. Targeting of this exon 5 transcript with a second shRNA resulted in inhibition of virus replication at both low and high m.o.i. These studies indicate that IE-3 has a complex transcriptional profile and that shRNA targeting of this and other viral regulatory genes which produce multiple transcripts may have unexpected effects on virus replication.",{"EN":271},"The effect of murine cytomegalovirus IE-3 specific shRNA is dependent on intragenic target site due to multiple transcription initiation sites",{"VOID":273},"10.1186\u002F2042-4280-2-9","https:\u002F\u002Fherpesviridae.biomedcentral.com\u002Farticles\u002F10.1186\u002F2042-4280-2-9",[276,291,303],{"id":277,"sortIndex":203,"researcher":19,"roles":278,"affiliations":279,"properties":288},"6ff74e82-b1b7-4bb5-99e4-f215d1e4c595",[51],[280],{"id":19,"sortIndex":20,"affiliation":281,"properties":19},{"id":282,"createTime":283,"updateTime":283,"relativeEntities":284,"slug":19,"properties":285,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"566298a7-b2b0-47a1-a1b3-53c742b77340","2023-12-03T07:00:17.632+00:00",[],{"title":286},{"VI":287},"Department of Cellular Biology and Anatomy, Medical College of Georgia, Georgia Health Sciences University, Augusta, USA",{"title":289},{"VI":290},"Sally S Atherton",{"id":292,"sortIndex":20,"researcher":19,"roles":293,"affiliations":294,"properties":300},"2c2e9d9d-a5e1-46ae-af55-342f8b12ecdc",[51],[295],{"id":19,"sortIndex":20,"affiliation":296,"properties":19},{"id":282,"createTime":283,"updateTime":283,"relativeEntities":297,"slug":19,"properties":298,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":299},{"VI":287},{"title":301},{"VI":302},"Brendan Marshall",{"id":304,"sortIndex":216,"researcher":19,"roles":305,"affiliations":306,"properties":312},"20c51964-722d-4858-acc1-f3739eeff909",[51],[307],{"id":19,"sortIndex":20,"affiliation":308,"properties":19},{"id":282,"createTime":283,"updateTime":283,"relativeEntities":309,"slug":19,"properties":310,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":311},{"VI":287},{"title":313},{"VI":314},"Ming Zhang",{"url":274,"publisher":316,"properties":325},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":317,"slug":10,"properties":318,"entityType":17,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"subjectFields":322,"manageAffiliations":323,"indexDatabases":324,"url":19,"thumbnailPath":19,"statistic":19,"gsStatistic":19,"type":19,"analyzePriority":19},[],{"issn":319,"title":320,"url":321},{"VOID":13},{"EN":10},{"VOID":16},[],[],[],{"volume":326,"pages":328},{"VOID":327},"2",{"VOID":329},"1-11","2011-09-18",2011,{"id":333,"createTime":334,"updateTime":335,"relativeEntities":336,"slug":337,"properties":338,"entityType":43,"verifyStatus":44,"verifyTime":335,"verifyNote":45,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"primaryUrl":347,"fullTextUrl":19,"authors":348,"publicationType":240,"publisherRelationship":390,"citationCount":19,"citationInfo":19,"publishDate":256,"publishYear":257,"citationAnalyzeStatus":18,"lastCitationAnalyze":19,"indexDatabases":19,"openAccess":19,"references":19,"isForceReanalyzing":258},"13da6ea4-d02b-4fa5-a639-8d7ec9a0d2eb","2024-01-17T04:09:43.758+00:00","2025-02-01T22:35:52.928+00:00",[],"Epstein-Barr-virus-genetics-talking-about-the-BAC-generation",{"references":339,"abstract":341,"title":343,"doi":345},{"VOID":340},"Heller M, Dambaugh T, Kieff E: Epstein-Barr virus DNA. 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Nat Genet. 2004, 36: 1099-1104. 10.1038\u002Fng1424.\nBhende PM, Seaman WT, Delecluse HJ, Kenney SC: BZLF1 activation of the methylated form of the BRLF1 immediate-early promoter is regulated by BZLF1 residue 186. J Virol. 2005, 79: 7338-7348. 10.1128\u002FJVI.79.12.7338-7348.2005.\nSchelcher C, Valencia S, Delecluse HJ, Hicks M, Sinclair AJ: Mutation of a single amino acid residue in the basic region of the Epstein-Barr virus (EBV) lytic cycle switch protein Zta (BZLF1) prevents reactivation of EBV from latency. J Virol. 2005, 79: 13822-13828. 10.1128\u002FJVI.79.21.13822-13828.2005.\nHeston L, El-Guindy A, Countryman J, Dela Cruz C, Delecluse HJ, Miller G: Amino acids in the basic domain of Epstein-Barr virus ZEBRA protein play distinct roles in DNA binding, activation of early lytic gene expression, and promotion of viral DNA replication. J Virol. 2006, 80: 9115-9133. 10.1128\u002FJVI.00909-06.\nEl-Guindy A, Heston L, Delecluse HJ, Miller G: Phosphoacceptor site S173 in the regulatory domain of Epstein-Barr Virus ZEBRA protein is required for lytic DNA replication but not for activation of viral early genes. J Virol. 2007, 81: 3303-3316. 10.1128\u002FJVI.02445-06.\nHong GK, Kumar P, Wang L, Damania B, Gulley ML, Delecluse HJ, Polverini PJ, Kenney SC: Epstein-Barr virus lytic infection is required for efficient production of the angiogenesis factor vascular endothelial growth factor in lymphoblastoid cell lines. J Virol. 2005, 79: 13984-13992. 10.1128\u002FJVI.79.22.13984-13992.2005.\nPark R, Heston L, Shedd D, Delecluse HJ, Miller G: Mutations of amino acids in the DNA-recognition domain of Epstein-Barr virus ZEBRA protein alter its sub-nuclear localization and affect formation of replication compartments. Virology. 2008, 382: 145-162. 10.1016\u002Fj.virol.2008.09.009.\nJones RJ, Seaman WT, Feng WH, Barlow E, Dickerson S, Delecluse HJ, Kenney SC: Roles of lytic viral infection and IL-6 in early versus late passage lymphoblastoid cell lines and EBV-associated lymphoproliferative disease. Int J Cancer. 2007, 121: 1274-1281. 10.1002\u002Fijc.22839.\nPudney VA, Leese AM, Rickinson AB, Hislop AD: CD8+ immunodominance among Epstein-Barr virus lytic cycle antigens directly reflects the efficiency of antigen presentation in lytically infected cells. J Exp Med. 2005, 201: 349-360. 10.1084\u002Fjem.20041542.\nZuo J, Currin A, Griffin BD, Shannon-Lowe C, Thomas WA, Ressing ME, Wiertz EJ, Rowe M: The Epstein-Barr virus G-protein-coupled receptor contributes to immune evasion by targeting MHC class I molecules for degradation. PLoS Pathog. 2009, 5: e1000255-10.1371\u002Fjournal.ppat.1000255.\nHumme S, Reisbach G, Feederle R, Delecluse HJ, Bousset K, Hammerschmidt W, Schepers A: The EBV nuclear antigen 1 (EBNA1) enhances B cell immortalization several thousandfold. Proc Natl Acad Sci USA. 2003, 100: 10989-10994. 10.1073\u002Fpnas.1832776100.\nAltmann M, Pich D, Ruiss R, Wang J, Sugden B, Hammerschmidt W: Transcriptional activation by EBV nuclear antigen 1 is essential for the expression of EBV's transforming genes. Proc Natl Acad Sci USA. 2006, 103: 14188-14193. 10.1073\u002Fpnas.0605985103.\nAltmann M, Hammerschmidt W: Epstein-Barr virus provides a new paradigm: a requirement for the immediate inhibition of apoptosis. PLoS Biol. 2005, 3: e404-10.1371\u002Fjournal.pbio.0030404.\nRowe M, Glaunsinger B, van Leeuwen D, Zuo J, Sweetman D, Ganem D, Middeldorp J, Wiertz EJ, Ressing ME: Host shutoff during productive Epstein-Barr virus infection is mediated by BGLF5 and may contribute to immune evasion. Proc Natl Acad Sci USA. 2007, 104: 3366-3371. 10.1073\u002Fpnas.0611128104.\nZuo J, Thomas W, van Leeuwen D, Middeldorp JM, Wiertz EJ, Ressing ME, Rowe M: The DNase of gammaherpesviruses impairs recognition by virus-specific CD8+ T cells through an additional host shutoff function. J Virol. 2008, 82: 2385-2393. 10.1128\u002FJVI.01946-07.\nRessing ME, van Leeuwen D, Verreck FA, Keating S, Gomez R, Franken KL, Ottenhoff TH, Spriggs M, Schumacher TN, Hutt-Fletcher LM, et al: Epstein-Barr virus gp42 is posttranslationally modified to produce soluble gp42 that mediates HLA class II immune evasion. J Virol. 2005, 79: 841-852. 10.1128\u002FJVI.79.2.841-852.2005.\nChackerian B: Virus-like particles: flexible platforms for vaccine development. Expert Rev Vaccines. 2007, 6: 381-390. 10.1586\u002F14760584.6.3.381.\nRamqvist T, Andreasson K, Dalianis T: Vaccination, immune and gene therapy based on virus-like particles against viral infections and cancer. Expert Opin Biol Ther. 2007, 7: 997-1007. 10.1517\u002F14712598.7.7.997.\nDargan DJ, Patel AH, Subak-Sharpe JH: PREPs: herpes simplex virus type 1-specific particles produced by infected cells when viral DNA replication is blocked. J Virol. 1995, 69: 4924-4932.\nMocarski ES, Shenk T, Pass RF: Cytomegaloviruses. Fields Virology Volume 2. Edited by: Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE. 2007, Philadelphia: Lippincott Williams &Wilkins, 2: 2701-2772. 5\nFeederle R, Shannon-Lowe C, Baldwin G, Delecluse HJ: Defective infectious particles and rare packaged genomes produced by cells carrying terminal-repeat-negative Epstein-Barr virus. J Virol. 2005, 79: 7641-7647. 10.1128\u002FJVI.79.12.7641-7647.2005.\nAdhikary D, Behrends U, Feederle R, Delecluse HJ, Mautner J: Standardized and highly efficient expansion of Epstein-Barr virus-specific CD4+ T cells by using virus-like particles. J Virol. 2008, 82: 3903-3911. 10.1128\u002FJVI.02227-07.\nTanaka M, Kagawa H, Yamanashi Y, Sata T, Kawaguchi Y: Construction of an excisable bacterial artificial chromosome containing a full-length infectious clone of herpes simplex virus type 1: viruses reconstituted from the clone exhibit wild-type properties in vitro and in vivo. J Virol. 2003, 77: 1382-1391. 10.1128\u002FJVI.77.2.1382-1391.2003.\nTischer BK, Kaufer BB, Sommer M, Wussow F, Arvin AM, Osterrieder N: A self-excisable infectious bacterial artificial chromosome clone of varicella-zoster virus allows analysis of the essential tegument protein encoded by ORF9. J Virol. 2007, 81: 13200-13208. 10.1128\u002FJVI.01148-07.\nZhou F, Li Q, Wong SW, Gao SJ: Autoexcision of bacterial artificial chromosome facilitated by terminal repeat-mediated homologous recombination: a novel approach for generating traceless genetic mutants of herpesviruses. J Virol. 2010, 84: 2871-2880. 10.1128\u002FJVI.01734-09.\nGranato M, Feederle R, Farina A, Gonnella R, Santarelli R, Hub B, Faggioni A, Delecluse HJ: Deletion of Epstein-Barr virus BFLF2 leads to impaired viral DNA packaging and primary egress as well as to the production of defective viral particles. J Virol. 2008, 82: 4042-4051. 10.1128\u002FJVI.02436-07.\nFarina A, Feederle R, Raffa S, Gonnella R, Santarelli R, Frati L, Angeloni A, Torrisi MR, Faggioni A, Delecluse HJ: BFRF1 of Epstein-Barr virus is essential for efficient primary viral envelopment and egress. J Virol. 2005, 79: 3703-3712. 10.1128\u002FJVI.79.6.3703-3712.2005.\nMurata T, Isomura H, Yamashita Y, Toyama S, Sato Y, Nakayama S, Kudoh A, Iwahori S, Kanda T, Tsurumi T: Efficient production of infectious viruses requires enzymatic activity of Epstein-Barr virus protein kinase. Virology. 2009, 389: 75-81. 10.1016\u002Fj.virol.2009.04.007.\nMeng Q, Hagemeier SR, Kuny CV, Kalejta RF, Kenney SC: Simian virus 40 T\u002Ft antigens and lamin A\u002FC small interfering RNA rescue the phenotype of an Epstein-Barr virus protein kinase (BGLF4) mutant. J Virol. 2010, 84: 4524-4533. 10.1128\u002FJVI.02456-09.\nFeederle R, Bannert H, Lips H, Muller-Lantzsch N, Delecluse HJ: The Epstein-Barr virus alkaline exonuclease BGLF5 serves pleiotropic functions in virus replication. J Virol. 2009, 83: 4952-4962. 10.1128\u002FJVI.00170-09.\nNeuhierl B, Delecluse HJ: The Epstein-Barr virus BMRF1 gene is essential for lytic virus replication. J Virol. 2006, 80: 5078-5081. 10.1128\u002FJVI.80.10.5078-5081.2006.\nNakayama S, Murata T, Murayama K, Yasui Y, Sato Y, Kudoh A, Iwahori S, Isomura H, Kanda T, Tsurumi T: Epstein-Barr virus polymerase processivity factor enhances BALF2 promoter transcription as a coactivator for the BZLF1 immediate-early protein. J Biol Chem. 2009, 284: 21557-21568. 10.1074\u002Fjbc.M109.015685.\nFeederle R, Neuhierl B, Baldwin G, Bannert H, Hub B, Mautner J, Behrends U, Delecluse HJ: Epstein-Barr virus BNRF1 protein allows efficient transfer from the endosomal compartment to the nucleus of primary B lymphocytes. J Virol. 2006, 80: 9435-9443. 10.1128\u002FJVI.00473-06.\nYu X, Wang Z, Mertz JE: ZEB1 regulates the latent-lytic switch in infection by Epstein-Barr virus. PLoS Pathog. 2007, 3: e194-10.1371\u002Fjournal.ppat.0030194.\nKelly GL, Milner AE, Tierney RJ, Croom-Carter DS, Altmann M, Hammerschmidt W, Bell AI, Rickinson AB: Epstein-Barr virus nuclear antigen 2 (EBNA2) gene deletion is consistently linked with EBNA3A, -3B, and -3C expression in Burkitt's lymphoma cells and with increased resistance to apoptosis. J Virol. 2005, 79: 10709-10717. 10.1128\u002FJVI.79.16.10709-10717.2005.\nSkalska L, White RE, Franz M, Ruhmann M, Allday MJ: Epigenetic repression of p16(INK4A) by latent Epstein-Barr virus requires the interaction of EBNA3A and EBNA3C with CtBP. PLoS Pathog. 2010, 6: e1000951-10.1371\u002Fjournal.ppat.1000951.\nHertle ML, Popp C, Petermann S, Maier S, Kremmer E, Lang R, Mages J, Kempkes B: Differential gene expression patterns of EBV infected EBNA-3A positive and negative human B lymphocytes. PLoS Pathog. 2009, 5: e1000506-10.1371\u002Fjournal.ppat.1000506.\nMaruo S, Wu Y, Ishikawa S, Kanda T, Iwakiri D, Takada K: Epstein-Barr virus nuclear protein EBNA3C is required for cell cycle progression and growth maintenance of lymphoblastoid cells. Proc Natl Acad Sci USA. 2006, 103: 19500-19505. 10.1073\u002Fpnas.0604919104.\nDirmeier U, Neuhierl B, Kilger E, Reisbach G, Sandberg ML, Hammerschmidt W: Latent membrane protein 1 is critical for efficient growth transformation of human B cells by epstein-barr virus. Cancer Res. 2003, 63: 2982-2989.\nMancao C, Hammerschmidt W: Epstein-Barr virus latent membrane protein 2A is a B-cell receptor mimic and essential for B-cell survival. Blood. 2007, 110: 3715-3721. 10.1182\u002Fblood-2007-05-090142.\nFeederle R, Delecluse HJ: Low level of lytic replication in a recombinant Epstein-Barr virus carrying an origin of replication devoid of BZLF1-binding sites. J Virol. 2004, 78: 12082-12084. 10.1128\u002FJVI.78.21.12082-12084.2004.\nChau CM, Zhang XY, McMahon SB, Lieberman PM: Regulation of Epstein-Barr virus latency type by the chromatin boundary factor CTCF. J Virol. 2006, 80: 5723-5732. 10.1128\u002FJVI.00025-06.\nHutzinger R, Feederle R, Mrazek J, Schiefermeier N, Balwierz PJ, Zavolan M, Polacek N, Delecluse HJ, Huttenhofer A: Expression and processing of a small nucleolar RNA from the Epstein-Barr virus genome. PLoS Pathog. 2009, 5: e1000547-10.1371\u002Fjournal.ppat.1000547.\nDelecluse HJ, Pich D, Hilsendegen T, Baum C, Hammerschmidt W: A first-generation packaging cell line for Epstein-Barr virus-derived vectors. Proc Natl Acad Sci USA. 1999, 96: 5188-5193. 10.1073\u002Fpnas.96.9.5188.",{"EN":342},"Genetic mutant organisms pervade all areas of Biology. Early on, herpesviruses (HV) were found to be amenable to genetic analysis using homologous recombination techniques in eukaryotic cells. More recently, HV genomes cloned onto a bacterial artificial chromosome (BAC) have become available. HV BACs can be easily modified in E.coli and reintroduced in eukaryotic cells to produce infectious viruses. Mutants derived from HV BACs have been used both to understand the functions of all types of genetic elements present on the virus genome, but also to generate mutants with potentially medically relevant properties such as preventative vaccines. Here we retrace the development of the BAC technology applied to the Epstein-Barr virus (EBV) and review the strategies available for the construction of mutants. We expand on the appropriate controls required for proper use of the EBV BACs, and on the technical hurdles researchers face in working with these recombinants. We then discuss how further technological developments might successfully overcome these difficulties. Finally, we catalog the EBV BAC mutants that are currently available and illustrate their contributions to the field using a few representative examples.",{"EN":344},"Epstein-Barr virus genetics: talking about the BAC generation",{"VOID":346},"10.1186\u002F2042-4280-1-6","https:\u002F\u002Fherpesviridae.biomedcentral.com\u002Farticles\u002F10.1186\u002F2042-4280-1-6",[349,366,378],{"id":350,"sortIndex":216,"researcher":19,"roles":351,"affiliations":352,"properties":363},"8a0ff82f-3c4e-4b42-b9d9-7031b7b1fa1a",[51],[353],{"id":19,"sortIndex":20,"affiliation":354,"properties":19},{"id":355,"createTime":356,"updateTime":357,"relativeEntities":358,"slug":359,"properties":360,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"5b2ab270-93c8-43cc-bf48-7b1533a83f7e","2023-12-11T11:28:01.723+00:00","2024-12-05T10:06:34.635+00:00",[],"German-Cancer-Research-Centre-Heidelberg-Germany",{"title":361},{"VI":362},"German Cancer Research Centre, Heidelberg, Germany",{"title":364},{"VI":365},"Emmalene J Bartlett",{"id":367,"sortIndex":20,"researcher":19,"roles":368,"affiliations":369,"properties":375},"a4f77227-1c0e-41db-80b9-89fdf5b6a859",[51],[370],{"id":19,"sortIndex":20,"affiliation":371,"properties":19},{"id":355,"createTime":356,"updateTime":357,"relativeEntities":372,"slug":359,"properties":373,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":374},{"VI":362},{"title":376},{"VI":377},"Regina Feederle",{"id":379,"sortIndex":203,"researcher":19,"roles":380,"affiliations":381,"properties":387},"0dc07eef-1088-4342-a8b2-43eb23674d35",[51],[382],{"id":19,"sortIndex":20,"affiliation":383,"properties":19},{"id":355,"createTime":356,"updateTime":357,"relativeEntities":384,"slug":359,"properties":385,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":386},{"VI":362},{"title":388},{"VI":389},"Henri-Jacques Delecluse",{"url":347,"publisher":391,"properties":400},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":392,"slug":10,"properties":393,"entityType":17,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"subjectFields":397,"manageAffiliations":398,"indexDatabases":399,"url":19,"thumbnailPath":19,"statistic":19,"gsStatistic":19,"type":19,"analyzePriority":19},[],{"issn":394,"title":395,"url":396},{"VOID":13},{"EN":10},{"VOID":16},[],[],[],{"volume":401,"pages":402},{"VOID":253},{"VOID":403},"1-13",{"id":405,"createTime":406,"updateTime":406,"relativeEntities":407,"slug":19,"properties":408,"entityType":43,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"primaryUrl":417,"fullTextUrl":19,"authors":418,"publicationType":240,"publisherRelationship":470,"citationCount":19,"citationInfo":19,"publishDate":484,"publishYear":485,"citationAnalyzeStatus":18,"lastCitationAnalyze":19,"indexDatabases":19,"openAccess":19,"references":19,"isForceReanalyzing":258},"a31b058e-1ec9-46b8-b7bd-615603f9b54a","2024-02-13T20:04:29.136+00:00",[],{"references":409,"abstract":411,"title":413,"doi":415},{"VOID":410},"Rozenberg F, Deback C, Agut H: Herpes simplex encephalitis: from virus to therapy. 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J Gen Virol. 2006, 87: 1099-1108. 10.1099\u002Fvir.0.81541-0.\nThapa M, Welner RS, Pelayo R, Carr DJ: CXCL9 and CXCL10 expression are critical for control of genital herpes simplex virus type 2 infection through mobilization of HSV-specific CTL and NK cells to the nervous system. J Immunol. 2008, 180: 1098-1106.\nLiu T, Khanna KM, Chen X, Fink DJ, Hendricks RL: CD8(+) T cells can block herpes simplex virus type 1 (HSV-1) reactivation from latency in sensory neurons. J Exp Med. 2000, 191: 1459-1466. 10.1084\u002Fjem.191.9.1459.\nRager-Zisman B, Quan PC, Rosner M, Moller JR, Bloom BR: Role of NK cells in protection of mice against herpes simplex virus-1 infection. J Immunol. 1987, 138: 884-888.\nThapa M, Kuziel WA, Carr DJ: Susceptibility of CCR5-deficient mice to genital herpes simplex virus type 2 is linked to NK cell mobilization. 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Rev Med Virol. 2012, 22: 106-121. 10.1002\u002Frmv.716.\nKurt-Jones EA, Chan M, Zhou S, Wang J, Reed G, Bronson R, et al: Herpes simplex virus 1 interaction with Toll-like receptor 2 contributes to lethal encephalitis. Proc Natl Acad Sci U S A. 2004, 101: 1315-1320. 10.1073\u002Fpnas.0308057100.\nAravalli RN, Hu S, Rowen TN, Palmquist JM, Lokensgard JR: Cutting Edge: TLR2-Mediated Proinflammatory Cytokine and Chemokine Production by Microglial Cells in Response to Herpes Simplex Virus. J Immunol. 2005, 175: 4189-4193.\nLeoni V, Gianni T, Salvioli S, Campadelli-Fiume G: Herpes Simplex Virus Glycoproteins gH\u002FgL and gB Bind Toll-Like Receptor 2, and Soluble gH\u002FgL Is Sufficient To Activate NF-kappaB. J Virol. 2012, 86: 6555-6562. 10.1128\u002FJVI.00295-12.\nZhang SY, Jouanguy E, Ugolini S, Smahi A, Elain G, Romero P, et al: TLR3 deficiency in patients with herpes simplex encephalitis. Science. 2007, 317: 1522-1527. 10.1126\u002Fscience.1139522.\nLund J, Sato A, Akira S, Medzhitov R, Iwasaki A: Toll-like receptor 9-mediated recognition of Herpes simplex virus-2 by plasmacytoid dendritic cells. J Exp Med. 2003, 198: 513-520. 10.1084\u002Fjem.20030162.\nMalmgaard L, Melchjorsen J, Bowie AG, Mogensen SC, Paludan SR: Viral activation of macrophages through TLR-dependent and -independent pathways. J Immunol. 2004, 173: 6890-6898.\nHochrein H, Schlatter B, O'Keeffe M, Wagner C, Schmitz F, Schiemann M, et al: Herpes simplex virus type-1 induces IFN-alpha production via Toll-like receptor 9-dependent and -independent pathways. Proc Natl Acad Sci U S A. 2004, 101: 11416-11421. 10.1073\u002Fpnas.0403555101.\nMelchjorsen J, Rintahaka J, Soby S, Horan KA, Poltajainen A, Ostergaard L, et al: Early innate recognition of herpes simplex virus in human primary macrophages is mediated via the MDA5\u002FMAVS-dependent and MDA5\u002FMAVS\u002FRNA polymerase III-independent pathways. J Virol. 2010, 84: 11350-11358. 10.1128\u002FJVI.01106-10.\nHolm CK, Jensen SB, Jakobsen MR, Cheshenko N, Horan KA, Moeller HB, et al: Virus-cell fusion as a trigger of innate immunity dependent on the adaptor STING. Nat Immunol. 2012, 13: 737-743. 10.1038\u002Fni.2350.\nUnterholzner L, Keating SE, Baran M, Horan KA, Jensen SB, Sharma S, et al: IFI16 is an innate immune sensor for intracellular DNA. Nat Immunol. 2010, 11: 997-1004. 10.1038\u002Fni.1932.\nRasmussen SB, Sorensen LN, Malmgaard L, Ank N, Baines JD, Chen ZJ, et al: Type I IFN production during herpes simplex virus infection is controlled by cell-type specific viral recognition through TLR9, the MAVS pathway, and novel recognition systems. J Virol. 2007, 81: 13315-13324. 10.1128\u002FJVI.01167-07.\nMelchjorsen J, Kristiansen H, Christiansen R, Rintahaka J, Matikainen S, Paludan SR, et al: Differential Regulation of the OASL and OAS1 Genes in Response to Viral Infections. J Interferon Cytokine Res. 2009, 29: 199-207. 10.1089\u002Fjir.2008.0050.\nMelchjorsen J, Matikainen S: Paludan SR:Activation and Evasion of Innate Antiviral Immunity by Herpes Simplex Virus. Viruses. 2009, 1: 737-759. 10.3390\u002Fv1030737.\nPaladino P, Mossman KL: Mechanisms Employed by HSV-1 to Inhibit the Interferon Response. J Interferon Cytokine Res. 2009, 29: 599-607. 10.1089\u002Fjir.2009.0074.\nTakaoka A, Wang Z, Choi MK, Yanai H, Negishi H, Ban T, et al: DAI (DLM-1\u002FZBP1) is a cytosolic DNA sensor and an activator of innate immune response. Nature. 2007, 448: 501-505. 10.1038\u002Fnature06013.\nCiesielski CJ, Andreakos E, Foxwell BM, Feldmann M: TNFalpha-induced macrophage chemokine secretion is more dependent on NF-kappaB expression than lipopolysaccharides-induced macrophage chemokine secretion. Eur J Immunol. 2002, 32: 2037-2045. 10.1002\u002F1521-4141(200207)32:7\u003C2037::AID-IMMU2037>3.0.CO;2-I.\nGariano GR, Dell'Oste V, Bronzini M, Gatti D, Luganini A, Andrea MD, et al: The intracellular DNA sensor IFI16 gene acts as restriction factor for human cytomegalovirus replication. PLoS Pathog. 2012, 8: e1002498-10.1371\u002Fjournal.ppat.1002498.\nCollins SE, Noyce RS, Mossman KL: Innate cellular response to virus particle entry requires IRF3 but not virus replication. J Virol. 2004, 78: 1706-1717. 10.1128\u002FJVI.78.4.1706-1717.2004.\nZhang Z, Yuan B, Bao M, Lu N, Kim T, Liu YJ: The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells. Nat Immunol. 2011, 12: 959-965. 10.1038\u002Fni.2091.\nMiyashita M, Oshiumi H, Matsumoto M, Seya T: DDX60, a DExD\u002FH box helicase, is a novel antiviral factor promoting RIG-I-like receptor-mediated signaling. Mol Cell Biol. 2011, 31: 3802-3819. 10.1128\u002FMCB.01368-10.\nKim T, Pazhoor S, Bao M, Zhang Z, Hanabuchi S, Facchinetti V, et al: Aspartate-glutamate-alanine-histidine box motif (DEAH)\u002FRNA helicase A helicases sense microbial DNA in human plasmacytoid dendritic cells. Proc Natl Acad Sci U S A. 2010, 107: 15181-15186. 10.1073\u002Fpnas.1006539107.\nZhang X, Brann TW, Zhou M, Yang J, Oguariri RM, Lidie KB, et al: Cutting edge: Ku70 is a novel cytosolic DNA sensor that induces type III rather than type I IFN. J Immunol. 2011, 186: 4541-4545. 10.4049\u002Fjimmunol.1003389.\nIwasaki A: Antiviral immune responses in the genital tract: clues for vaccines. Nat Rev Immunol. 2010, 10: 699-711. 10.1038\u002Fnri2836.\nBernstein DI, Earwood JD, Bravo FJ, Cohen GH, Eisenberg RJ, Clark JR, et al: Effects of herpes simplex virus type 2 glycoprotein vaccines and CLDC adjuvant on genital herpes infection in the guinea pig. Vaccine. 2011, 29: 2071-2078. 10.1016\u002Fj.vaccine.2011.01.005.\nBernstein DI, Farley N, Bravo FJ, Earwood J, McNeal M, Fairman J, et al: The adjuvant CLDC increases protection of a herpes simplex type 2 glycoprotein D vaccine in guinea pigs. Vaccine. 2010, 28: 3748-3753. 10.1016\u002Fj.vaccine.2009.10.025.\nBernstein DI, Cardin RD, Bravo FJ, Strasser JE, Farley N, Chalk C, et al: Potent adjuvant activity of cationic liposome-DNA complexes for genital herpes vaccines. Clin Vaccine Immunol. 2009, 16: 699-705. 10.1128\u002FCVI.00370-08.",{"EN":412},"Innate recognition is essential in the antiviral response against infection by herpes simplex virus (HSV). Chemokines are important for control of HSV via recruitment of natural killer cells, T lymphocytes, and antigen-presenting cells. We previously found that early HSV-1-mediated chemokine responses are not dependent on TLR2 and TLR9 in human macrophages. Here, we investigated the role of the recently identified innate IFN-inducible DNA receptor IFI16 during HSV-1 infection in human macrophages. Peripheral blood mononuclear cells were purified from buffy coats and monocytes were differentiated to macrophages. Macrophages infected with HSV-1 were analyzed using siRNA-mediated knock-down of IFI16 by real-time PCR, ELISA, and Western blotting. We determined that both CXCL10 and CCL3 are induced independent of HSV-1 replication. IFI16 mediates CCL3 mRNA accumulation during early HSV-1 infection. In contrast, CXCL10 was induced independently of IFI16. Our data provide the first evidence of HSV-1-induced innate immune responses via IFI16 in human primary macrophages. In addition, the data suggest that at least one additional unidentified receptor or innate sensing mechanism is involved in recognizing HSV-1 prior to viral replication.",{"EN":414},"HSV-1-induced chemokine expression via IFI16-dependent and IFI16-independent pathways in human monocyte-derived macrophages",{"VOID":416},"10.1186\u002F2042-4280-3-6","https:\u002F\u002Fherpesviridae.biomedcentral.com\u002Farticles\u002F10.1186\u002F2042-4280-3-6",[419,434,446,458],{"id":420,"sortIndex":216,"researcher":19,"roles":421,"affiliations":422,"properties":431},"e70943a7-24ba-4ae9-b981-006a496fbba3",[51],[423],{"id":19,"sortIndex":20,"affiliation":424,"properties":19},{"id":425,"createTime":426,"updateTime":426,"relativeEntities":427,"slug":19,"properties":428,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"48d9421d-a331-419c-b4cb-5a442ce0e4b9","2023-12-28T13:39:44.582+00:00",[],{"title":429},{"VI":430},"Department of Infectious Diseases, Aarhus University Hospital, Aarhus N, Denmark",{"title":432},{"VI":433},"Rune R Laursen",{"id":435,"sortIndex":203,"researcher":19,"roles":436,"affiliations":437,"properties":443},"27b80771-65c7-4e3e-9bd0-b899315a51ab",[51],[438],{"id":19,"sortIndex":20,"affiliation":439,"properties":19},{"id":425,"createTime":426,"updateTime":426,"relativeEntities":440,"slug":19,"properties":441,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":442},{"VI":430},{"title":444},{"VI":445},"Lars Østergaard",{"id":447,"sortIndex":20,"researcher":19,"roles":448,"affiliations":449,"properties":455},"178cb459-fd72-4381-b4c6-62603334745f",[51],[450],{"id":19,"sortIndex":20,"affiliation":451,"properties":19},{"id":425,"createTime":426,"updateTime":426,"relativeEntities":452,"slug":19,"properties":453,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":454},{"VI":430},{"title":456},{"VI":457},"Stine Søby",{"id":459,"sortIndex":67,"researcher":19,"roles":460,"affiliations":461,"properties":467},"2cb59dff-31a0-4318-9cfb-542ebf3c4941",[51],[462],{"id":19,"sortIndex":20,"affiliation":463,"properties":19},{"id":425,"createTime":426,"updateTime":426,"relativeEntities":464,"slug":19,"properties":465,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":466},{"VI":430},{"title":468},{"VI":469},"Jesper Melchjorsen",{"url":417,"publisher":471,"properties":480},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":472,"slug":10,"properties":473,"entityType":17,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"subjectFields":477,"manageAffiliations":478,"indexDatabases":479,"url":19,"thumbnailPath":19,"statistic":19,"gsStatistic":19,"type":19,"analyzePriority":19},[],{"issn":474,"title":475,"url":476},{"VOID":13},{"EN":10},{"VOID":16},[],[],[],{"volume":481,"pages":483},{"VOID":482},"3",{"VOID":255},"2012-10-14",2012,{"id":487,"createTime":488,"updateTime":488,"relativeEntities":489,"slug":19,"properties":490,"entityType":43,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"primaryUrl":499,"fullTextUrl":19,"authors":500,"publicationType":240,"publisherRelationship":544,"citationCount":19,"citationInfo":19,"publishDate":558,"publishYear":485,"citationAnalyzeStatus":18,"lastCitationAnalyze":19,"indexDatabases":19,"openAccess":19,"references":19,"isForceReanalyzing":258},"6908a2c7-8ff0-4b43-b5f8-069e6c690d6b","2023-12-28T19:35:41.875+00:00",[],{"references":491,"abstract":493,"title":495,"doi":497},{"VOID":492},"Cannon MJ, Davis KF: Washing our hands of the congenital cytomegalovirus disease epidemic. BMC Public Health. 2005, 5: 70-10.1186\u002F1471-2458-5-70.\nCannon MJ: Congenital cytomegalovirus (CMV) epidemiology and awareness. J Clin Virol. 2009, 46 (Suppl 4): S6-S10.\nFowler KB, Stagno S, Pass RF: Maternal immunity and prevention of congenital cytomegalovirus infection. JAMA. 2003, 289 (8): 1008-1011. 10.1001\u002Fjama.289.8.1008.\nMendelson E, Aboudy Y, Smetana Z, Tepperberg M, Grossman Z: Laboratory assessment and diagnosis of congenital viral infections: Rubella, cytomegalovirus (CMV), varicella-zoster virus (VZV), herpes simplex virus (HSV), parvovirus B19 and human immunodeficiency virus (HIV). Reprod Toxicol. 2006, 21 (4): 350-382. 10.1016\u002Fj.reprotox.2006.02.001.\nBrennan DC: Cytomegalovirus in renal transplantation. J Am Soc Nephrol. 2001, 12 (4): 848-855.\nCDC. CMV: Intepretation of laboratory tests. http:\u002F\u002Fwww.cdc.gov\u002Fcmv\u002Fclinical\u002Flab-tests.html]. Accessed 2011 December 10\nRazonable RR: Cytomegalovirus infection after liver transplation:current concepts and challenges. World J Gastroent. 2008, 14 (31): 4849-4860. 10.3748\u002Fwjg.14.4849.\nKotton CN, Kumar D, Caliendo AM, et al: International consensus guidelines on the management of cytomegalovirus in solid organ transplantation. Transplantation. 2010, 89 (7): 779-795. 10.1097\u002FTP.0b013e3181cee42f.\nFielding K, Koba A, Grant AD, et al: Cytomegalovirus viremia as a risk factor for mortality prior to antiretroviral therapy among HIV-infected gold miners in South Africa. PLoS One. 2011, 6 (10): e25571-10.1371\u002Fjournal.pone.0025571.",{"EN":494},"Diagnosis of cytomegalovirus (CMV) infection is challenging because of the high rate of asymptomatic infection and the low specificity of associated symptoms and signs. As a result, laboratory testing is an essential aid in making an accurate diagnosis. The presence of CMV IgM is indicative of primary CMV infection. In pregnancy, diagnosis of primary infection is important because primary maternal infection increases fetal infection risk substantially. Fetal infection can result in serious sequelae ranging from neurological deficits to death. Diagnosis among the immunocompromised is also critical for the timely initiation of therapy that can reduce morbidity and mortality risk. The IMMULITE® 2000 CMV IgM assay qualitatively detects CMV IgM antibodies in human serum or plasma to aid in the diagnosis of current or recent CMV infection. To determine expected values in apparently healthy subjects, 136 samples were tested. Reproducibility, normal range, and method comparison studies were also performed to evaluate the assay's performance. The assay's reproducibility was evaluated across three sites. Seven hundred and eighteen (n = 718) individual patient serum samples, which included samples from CMV IgM-positive (n = 109, determined by the Abbott IMx CMV or the Diamedix CMV IgM assays), pregnant (n = 210), HIV-positive (n = 30), immunosuppressed (n = 102), and transplant patients (n = 17) and from patients with potentially cross-reacting conditions (n = 136) were evaluated in the method comparison study. The positive, negative, and overall agreement between the IMMULITE 2000 CMV IgM assay and the VIDAS CMV IgM assay (predicate assay) were determined. The assay demonstrated excellent reproducibility with a total CV of less than 10%. The positive, negative, and overall agreement between the IMMULITE 2000 assay and the VIDAS assay were > 95% for the method comparison samples. Among potentially cross-reactive samples, the overall agreement between the two assays was 96%. Similarly, among the immunocompromised and pregnant subjects, the overall agreement was ~96% and ~97%, respectively. The IMMULITE 2000 CMV IgM assay demonstrated excellent reproducibility, minimal cross-reactivity, and performance comparable to that of the VIDAS CMV IgM assay. It can aid in the diagnosis of acute CMV or recent CMV infection by qualitatively detecting the CMV IgM antibodies in human serum or plasma.",{"EN":496},"Evaluation of the IMMULITE®2000 CMV IgM assay",{"VOID":498},"10.1186\u002F2042-4280-3-2","https:\u002F\u002Fherpesviridae.biomedcentral.com\u002Farticles\u002F10.1186\u002F2042-4280-3-2",[501,516,532],{"id":502,"sortIndex":20,"researcher":19,"roles":503,"affiliations":504,"properties":513},"ba846e15-84d5-4520-89a1-40efea42224a",[51],[505],{"id":19,"sortIndex":20,"affiliation":506,"properties":19},{"id":507,"createTime":508,"updateTime":508,"relativeEntities":509,"slug":19,"properties":510,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"c1d53ca9-4036-4a4d-9d51-153f25a75b9f","2023-12-28T19:35:41.893+00:00",[],{"title":511},{"VI":512},"Siemens Healthcare Diagnostics, Los Angeles, USA",{"title":514},{"VI":515},"Tricia A Bal",{"id":517,"sortIndex":203,"researcher":19,"roles":518,"affiliations":519,"properties":529},"e5840fd2-4f9b-4209-854b-d89b0012efad",[51],[520],{"id":19,"sortIndex":20,"affiliation":521,"properties":19},{"id":522,"createTime":523,"updateTime":523,"relativeEntities":524,"slug":525,"properties":526,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"1853fe26-ed08-4c36-b4e6-0d8ec7227af3","2024-04-15T19:30:15.007+00:00",[],"University-of-Texas-MD-Anderson-Cancer-Center-Houston-USA",{"title":527},{"EN":528},"University of Texas MD Anderson Cancer Center, Houston, USA",{"title":530},{"VI":531},"Xiang Y Han",{"id":533,"sortIndex":216,"researcher":19,"roles":534,"affiliations":535,"properties":541},"a941cfe8-f3c6-4bac-9de7-dacdc34e9461",[51],[536],{"id":19,"sortIndex":20,"affiliation":537,"properties":19},{"id":507,"createTime":508,"updateTime":508,"relativeEntities":538,"slug":19,"properties":539,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":540},{"VI":512},{"title":542},{"VI":543},"Glenn Armstrong",{"url":499,"publisher":545,"properties":554},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":546,"slug":10,"properties":547,"entityType":17,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"subjectFields":551,"manageAffiliations":552,"indexDatabases":553,"url":19,"thumbnailPath":19,"statistic":19,"gsStatistic":19,"type":19,"analyzePriority":19},[],{"issn":548,"title":549,"url":550},{"VOID":13},{"EN":10},{"VOID":16},[],[],[],{"volume":555,"pages":556},{"VOID":482},{"VOID":557},"1-5","2012-02-29",{"id":560,"createTime":561,"updateTime":561,"relativeEntities":562,"slug":19,"properties":563,"entityType":43,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"primaryUrl":572,"fullTextUrl":19,"authors":573,"publicationType":240,"publisherRelationship":601,"citationCount":19,"citationInfo":19,"publishDate":615,"publishYear":331,"citationAnalyzeStatus":18,"lastCitationAnalyze":19,"indexDatabases":19,"openAccess":19,"references":19,"isForceReanalyzing":258},"532655ce-c467-4e10-b78b-4b994ce3eb9b","2024-01-26T19:34:42.908+00:00",[],{"references":564,"abstract":566,"title":568,"doi":570},{"VOID":565},"Pellet P, Roizman B: Herpesviridae: A Brief Introduction. Fields Virology. Edited by: Howley P. 2007, Philadelphia: Lippincott, 2480-2499. 5\nBresnahan WA, Shenk TE: UL82 virion protein activates expression of immediate early viral genes in human cytomegalovirus-infected cells. Proc Natl Acad Sci USA. 2000, 97: 14506-14511. 10.1073\u002Fpnas.97.26.14506.\nMoriuchi H, Moriuchi M, Straus SE, Cohen JI: Varicella-zoster virus open reading frame 10 protein, the herpes simplex virus VP16 homolog, transactivates herpesvirus immediate-early gene promoters. J Virol. 1993, 67: 2739-2746.\nWysocka J, Herr W: The herpes simplex virus VP16-induced complex: the makings of a regulatory switch. Trends Biochem Sci. 2003, 28: 294-304. 10.1016\u002FS0968-0004(03)00088-4.\nNicholson IP, Sutherland JS, Chaudry TN, Blewett EL, Barry PA, Nicholl MJ, Preston CM: Properties of virion transactivator proteins encoded by primate cytomegaloviruses. Virol J. 2009, 6: 65-10.1186\u002F1743-422X-6-65.\nSchreiber A, Harter G, Schubert A, Bunjes D, Mertens T, Michel D: Antiviral treatment of cytomegalovirus infection and resistant strains. Expert Opin Pharmacother. 2009, 10: 191-209. 10.1517\u002F14656560802678138.\nBillaud G, Thouvenot D, Morfin F: Drug targets in herpes simplex and Epstein Barr Virus infections. Infect Disord Drug Targets. 2009, 9: 117-125.\nRoizman B, Knipe D, Whitley R: Herpes Simplex Viruses. Fields Virology. Edited by: Howley P. 2007, Philadelphia: Lippincott, 2501-2601. 5\nCohen J, Straus S, Arvin A: Varicella-Zoster Virus Replication, Pathogenesis, and Management. Fields Virology. Edited by: Howley P. 2007, Philadelphia: Lippincott, 2773-2818. 5\nSinclair J: Human cytomegalovirus: Latency and reactivation in the myeloid lineage. J Clin Virol. 2008, 41: 180-185. 10.1016\u002Fj.jcv.2007.11.014.\nMendelson M, Monard S, Sissons P, Sinclair J: Detection of endogenous human cytomegalovirus in CD34+ bone marrow progenitors. J Gen Virol. 1996, 77 (Pt 12): 3099-3102. 10.1099\u002F0022-1317-77-12-3099.\nMocarski E, Shenk T, Pass R: Cytomegaloviruses. Fields Virology. Edited by: Howley P. 2007, Philadelphia: Lippincott, 2701-2772. 5\nDe Bolle L, Naesens L, De Clercq E: Update on human herpesvirus 6 biology, clinical features, and therapy. Clin Microbiol Rev. 2005, 18: 217-245. 10.1128\u002FCMR.18.1.217-245.2005.\nYamanishi K, Mori Y, Pellet P: Human Herpesviruses 6 and 7. Fields Virology. Edited by: Howley P. 2007, Philadelphia: Lippincott, 2820-2845. 5\nMiyake F, Yoshikawa T, Sun H, Kakimi A, Ohashi M, Akimoto S, Nishiyama Y, Asano Y: Latent infection of human herpesvirus 7 in CD4(+) T lymphocytes. J Med Virol. 2006, 78: 112-116. 10.1002\u002Fjmv.20511.\nColeman CB, Nealy MS, Tibbetts SA: Immature and transitional B cells are latency reservoirs for a gammaherpesvirus. J Virol. 2010, 84: 13045-13052. 10.1128\u002FJVI.01455-10.\nRickinson A, Kieff E: Epstein-Barr Virus. Fields Virology. Edited by: Howley P. 2007, Philadelphia: Lippincott, 2655-2700. 5\nGanem D: Kaposi's Sarcoma-associated Herpesvirus. Fields Virology. Edited by: Howley P. 2007, Philadelphia: Lippincott, 2848-2888. 5\nEfstathiou S, Preston CM: Towards an understanding of the molecular basis of herpes simplex virus latency. Virus Res. 2005, 111: 108-119. 10.1016\u002Fj.virusres.2005.04.017.\nBloom DC, Giordani NV, Kwiatkowski DL: Epigenetic regulation of latent HSV-1 gene expression. Biochim Biophys Acta. 2010, 1799: 246-256.\nKnipe DM, Cliffe A: Chromatin control of herpes simplex virus lytic and latent infection. Nat Rev Microbiol. 2008, 6: 211-221. 10.1038\u002Fnrmicro1794.\nKutluay SB, Triezenberg SJ: Role of chromatin during herpesvirus infections. Biochim Biophys Acta. 2009, 1790: 456-466.\nPerng GC, Jones C: Towards an understanding of the herpes simplex virus type 1 latency-reactivation cycle. Interdiscip Perspect Infect Dis. 2010, 2010: 262415-\nSissons JG, Bain M, Wills MR: Latency and reactivation of human cytomegalovirus. J Infect. 2002, 44: 73-77. 10.1053\u002Fjinf.2001.0948.\nBego MG, St Jeor S: Human cytomegalovirus infection of cells of hematopoietic origin: HCMV-induced immunosuppression, immune evasion, and latency. Exp Hematol. 2006, 34: 555-570. 10.1016\u002Fj.exphem.2005.11.012.\nSlobedman B, Cao JZ, Avdic S, Webster B, McAllery S, Cheung AK, Tan JC, Abendroth A: Human cytomegalovirus latent infection and associated viral gene expression. Future Microbiol. 2010, 5: 883-900. 10.2217\u002Ffmb.10.58.\nSinclair J: Chromatin structure regulates human cytomegalovirus gene expression during latency, reactivation and lytic infection. Biochim Biophys Acta. 2010, 1799: 286-295.\nSinclair J, Sissons P: Latency and reactivation of human cytomegalovirus. J Gen Virol. 2006, 87: 1763-1779. 10.1099\u002Fvir.0.81891-0.\nAmon W, Farrell PJ: Reactivation of Epstein-Barr virus from latency. Rev Med Virol. 2005, 15: 149-156. 10.1002\u002Frmv.456.\nYoung LS, Rickinson AB: Epstein-Barr virus: 40 years on. Nat Rev Cancer. 2004, 4: 757-768. 10.1038\u002Fnrc1452.\nTsurumi T, Fujita M, Kudoh A: Latent and lytic Epstein-Barr virus replication strategies. Rev Med Virol. 2005, 15: 3-15. 10.1002\u002Frmv.441.\nYoung LS, Dawson CW, Eliopoulos AG: The expression and function of Epstein-Barr virus encoded latent genes. Mol Pathol. 2000, 53: 238-247. 10.1136\u002Fmp.53.5.238.\nTempera I, Lieberman PM: Chromatin organization of gammaherpesvirus latent genomes. Biochim Biophys Acta. 2010, 1799: 236-245.\nCamarena V, Kobayashi M, Kim JY, Roehm P, Perez R, Gardner J, Wilson AC, Mohr I, Chao MV: Nature and duration of growth factor signaling through receptor tyrosine kinases regulates HSV-1 latency in neurons. Cell Host Microbe. 2010, 8: 320-330. 10.1016\u002Fj.chom.2010.09.007.\nDanaher RJ, Jacob RJ, Miller CS: Establishment of a quiescent herpes simplex virus type 1 infection in neurally-differentiated PC12 cells. J Neurovirol. 1999, 5: 258-267. 10.3109\u002F13550289909015812.\nJamieson DR, Robinson LH, Daksis JI, Nicholl MJ, Preston CM: Quiescent viral genomes in human fibroblasts after infection with herpes simplex virus type 1 Vmw65 mutants. J Gen Virol. 1995, 76 (Pt 6): 1417-1431. 10.1099\u002F0022-1317-76-6-1417.\nRussell J, Preston CM: An in vitro latency system for herpes simplex virus type 2. J Gen Virol. 1986, 67 (Pt 2): 397-403. 10.1099\u002F0022-1317-67-2-397.\nWilcox CL, Johnson EM: Nerve growth factor deprivation results in the reactivation of latent herpes simplex virus in vitro. J Virol. 1987, 61: 2311-2315.\nMa SD, Hegde S, Young KH, Sullivan R, Rajesh D, Zhou Y, Jankowska-Gan E, Burlingham WJ, Sun X, Gulley ML, et al: A new model of EBV infection reveals an important role for early lytic viral protein expression in the development of lymphomas. J Virol. 2010, 85: 165-177. 10.1128\u002FJVI.01512-10.\nSmith MS, Goldman DC, Bailey AS, Pfaffle DL, Kreklywich CN, Spencer DB, Othieno FA, Streblow DN, Garcia JV, Fleming WH, Nelson JA: Granulocyte-colony stimulating factor reactivates human cytomegalovirus in a latently infected humanized mouse model. Cell Host Microbe. 2010, 8: 284-291. 10.1016\u002Fj.chom.2010.08.001.\nAce CI, McKee TA, Ryan JM, Cameron JM, Preston CM: Construction and characterization of a herpes simplex virus type 1 mutant unable to transinduce immediate-early gene expression. J Virol. 1989, 63: 2260-2269.\nImai Y, Apakupakul K, Krause PR, Halford WP, Margolis TP: Investigation of the mechanism by which herpes simplex virus type 1 LAT sequences modulate preferential establishment of latent infection in mouse trigeminal ganglia. J Virol. 2009, 83: 7873-7882. 10.1128\u002FJVI.00043-09.\nMargolis TP, Imai Y, Yang L, Vallas V, Krause PR: Herpes simplex virus type 2 (HSV-2) establishes latent infection in a different population of ganglionic neurons than HSV-1: role of latency-associated transcripts. J Virol. 2007, 81: 1872-1878. 10.1128\u002FJVI.02110-06.\nProenca JT, Coleman HM, Connor V, Winton DJ, Efstathiou S: A historical analysis of herpes simplex virus promoter activation in vivo reveals distinct populations of latently infected neurones. J Gen Virol. 2008, 89: 2965-2974. 10.1099\u002Fvir.0.2008\u002F005066-0.\nMargolis TP, Dawson CR, LaVail JH: Herpes simplex viral infection of the mouse trigeminal ganglion. Immunohistochemical analysis of cell populations. Invest Ophthalmol Vis Sci. 1992, 33: 259-267.\nYang L, Voytek CC, Margolis TP: Immunohistochemical analysis of primary sensory neurons latently infected with herpes simplex virus type 1. J Virol. 2000, 74: 209-217. 10.1128\u002FJVI.74.1.209-217.2000.\nSawtell NM, Thompson RL: Herpes simplex virus type 1 latency-associated transcription unit promotes anatomical site-dependent establishment and reactivation from latency. J Virol. 1992, 66: 2157-2169.\nSpeck PG, Simmons A: Synchronous appearance of antigen-positive and latently infected neurons in spinal ganglia of mice infected with a virulent strain of herpes simplex virus. J Gen Virol. 1992, 73 (Pt 5): 1281-1285. 10.1099\u002F0022-1317-73-5-1281.\nLachmann RH, Sadarangani M, Atkinson HR, Efstathiou S: An analysis of herpes simplex virus gene expression during latency establishment and reactivation. J Gen Virol. 1999, 80 (Pt 5): 1271-1282.\nSawtell NM: Comprehensive quantification of herpes simplex virus latency at the single-cell level. J Virol. 1997, 71: 5423-5431.\nThompson RL, Sawtell NM: Replication of herpes simplex virus type 1 within trigeminal ganglia is required for high frequency but not high viral genome copy number latency. 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Herpesviral infections persist for the life of the infected host due in large part to the ability of these viruses to enter a non-productive, latent state in which viral gene expression is limited and immune detection and clearance is avoided. Periodically, the virus will reactivate and enter the lytic cycle, producing progeny virus that can spread within or to new hosts. Latency has been classically divided into establishment, maintenance, and reactivation phases. Here we focus on demonstrated and postulated molecular mechanisms leading to the establishment of latency for representative members of each human herpesvirus family. Maintenance and reactivation are also briefly discussed. In particular, the roles that tegument proteins may play during latency are highlighted. Finally, we introduce the term animation to describe the initiation of lytic phase gene expression from a latent herpesvirus genome, and discuss why this step should be separated, both molecularly and theoretically, from reactivation.",{"EN":569},"Tegument protein control of latent herpesvirus establishment and animation",{"VOID":571},"10.1186\u002F2042-4280-2-3","https:\u002F\u002Fherpesviridae.biomedcentral.com\u002Farticles\u002F10.1186\u002F2042-4280-2-3",[574,589],{"id":575,"sortIndex":216,"researcher":19,"roles":576,"affiliations":577,"properties":586},"70d9a921-b04e-49c5-b7de-a647bf6511aa",[51],[578],{"id":19,"sortIndex":20,"affiliation":579,"properties":19},{"id":580,"createTime":581,"updateTime":581,"relativeEntities":582,"slug":19,"properties":583,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"93491aab-6ee6-43f4-96cc-9ca4e9f9a91a","2024-01-26T19:34:42.934+00:00",[],{"title":584},{"VI":585},"Institute for Molecular Virology, McArdle Laboratory for Cancer Research, and Cell and Molecular Biology Training Program, University of Wisconsin-Madison, Madison, USA",{"title":587},{"VI":588},"Robert F 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in herpesvirus immune control and immune escape",{"VOID":634},"21429245",{"VOID":636},"10.1186\u002F2042-4280-2-2",[638],"EN","http:\u002F\u002Fherpesviridae.biomedcentral.com\u002Farticles\u002F10.1186\u002F2042-4280-2-2",[641,661,679],{"id":642,"sortIndex":203,"researcher":19,"roles":643,"affiliations":644,"properties":654},"b0e09898-61ef-4716-8dc8-5162a8d86d38",[],[645],{"id":19,"sortIndex":20,"affiliation":646,"properties":19},{"id":647,"createTime":648,"updateTime":648,"relativeEntities":649,"slug":650,"properties":651,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"cdec7aa4-1474-4640-9b4d-83be09e5d317","2024-04-15T19:10:41.916+00:00",[],"Viral-Immunobiology-Institute-of-Experimental-Immunology-University-Hospital-Z%C3%BCrich-Z%C3%BCrich-Switzerland",{"title":652},{"EN":653},"Viral Immunobiology, Institute of Experimental Immunology, University Hospital Zürich, Zürich, 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UK",{"openalex":675,"title":677},{"VOID":676},"A5084702053",{"EN":678},"Graham S. Taylor",{"id":680,"sortIndex":216,"researcher":19,"roles":681,"affiliations":682,"properties":692},"299393f2-614d-4c2b-80e1-5b9967494d30",[],[683],{"id":19,"sortIndex":20,"affiliation":684,"properties":19},{"id":685,"createTime":686,"updateTime":686,"relativeEntities":687,"slug":688,"properties":689,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"ad42d6ba-30f9-4773-ab36-072032da598f","2024-04-15T19:10:41.897+00:00",[],"Department-of-Pediatrics-Technische-Universit%C3%A4t-M%C3%BCnchen-and-Helmholtz-Zentrum-M%C3%BCnchen-German-Research-Center-for-Environmental-Health-Munich-Germany",{"title":690},{"EN":691},"Department of Pediatrics, Technische Universität München and Helmholtz Zentrum München, German Research Center for Environmental Health, Munich, Germany",{"openalex":693,"orcid":695,"title":697},{"VOID":694},"A5020317705",{"VOID":696},"https:\u002F\u002Forcid.org\u002F0000-0002-8680-1065",{"EN":698},"Josef Mautner",{"url":19,"publisher":700,"properties":19},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":701,"slug":10,"properties":702,"entityType":17,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"subjectFields":706,"manageAffiliations":707,"indexDatabases":708,"url":19,"thumbnailPath":19,"statistic":19,"gsStatistic":19,"type":19,"analyzePriority":19},[],{"issn":703,"title":704,"url":705},{"VOID":13},{"EN":10},{"VOID":16},[],[],[],16,{"total":709,"publishYear":19,"statisticByYear":711},{"2012":216,"2013":67,"2014":216,"2015":203,"2017":216,"2018":216,"2019":229},"2011-01-01",[],{"id":715,"createTime":716,"updateTime":717,"relativeEntities":718,"slug":719,"properties":720,"entityType":43,"verifyStatus":44,"verifyTime":717,"verifyNote":45,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"primaryUrl":729,"fullTextUrl":19,"authors":730,"publicationType":240,"publisherRelationship":780,"citationCount":19,"citationInfo":19,"publishDate":794,"publishYear":331,"citationAnalyzeStatus":18,"lastCitationAnalyze":19,"indexDatabases":19,"openAccess":19,"references":19,"isForceReanalyzing":258},"b8de91ad-a30d-48bd-ac24-85facd185725","2024-01-13T22:37:51.382+00:00","2025-02-11T19:00:01.769+00:00",[],"Deciphering-the-role-of-Epstein-Barr-virus-in-the-pathogenesis-of-T-and-NK-cell-lymphoproliferations",{"references":721,"abstract":723,"title":725,"doi":727},{"VOID":722},"Rickinson AB, Kieff E: Epstein-Barr virus. 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J Virol. 2008, 82 (4): 1739-1747. 10.1128\u002FJVI.01723-07.\nShah KM, Stewart SE, Wei W, Woodman CB, O'Neil JD, Dawson CW, Young LS: The EBV-encoded latent membrane proteins, LMP2A and LMP2B, limit the actions of interferon by targeting interferon receptors for degradation. Oncogene. 2009, 28 (44): 3903-3914. 10.1038\u002Fonc.2009.249.\nAllen MD, Young LS, Dawson CW: The Epstein-Barr Virus-Encoded LMP2A and LMP2B Proteins Promote Epithelial Cell Spreading and Motility. J Virol. 2005, 79 (3): 1789-1802. 10.1128\u002FJVI.79.3.1789-1802.2005.",{"EN":724},"Epstein-Barr virus (EBV) is a highly successful herpesvirus, colonizing more than 90% of the adult human population worldwide, although it is also associated with various malignant diseases. Primary infection is usually clinically silent, and subsequent establishment of latency in the memory B lymphocyte compartment allows persistence of the virus in the infected host for life. EBV is so markedly B-lymphotropic when exposed to human lymphocytes in vitro that the association of EBV with rare but distinct types of T and NK cell lymphoproliferations was quite unexpected. Whilst relatively rare, these EBV-associated T and NK lymphoproliferations can be therapeutically challenging and prognosis for the majority of patients is dismal. In this review, we summarize the current knowledge on the role of EBV in the pathogenesis of these tumours, and the implications for treatment.",{"EN":726},"Deciphering the role of Epstein-Barr virus in the pathogenesis of T and NK cell lymphoproliferations",{"VOID":728},"10.1186\u002F2042-4280-2-8","https:\u002F\u002Fherpesviridae.biomedcentral.com\u002Farticles\u002F10.1186\u002F2042-4280-2-8",[731,756,768],{"id":732,"sortIndex":20,"researcher":19,"roles":733,"affiliations":734,"properties":753},"59f1a667-9124-4221-becd-97c0a52820e8",[51],[735,743],{"id":19,"sortIndex":20,"affiliation":736,"properties":19},{"id":737,"createTime":738,"updateTime":738,"relativeEntities":739,"slug":19,"properties":740,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"f6a5fb43-c085-4204-b905-8df84c54b17f","2024-01-13T22:37:51.624+00:00",[],{"title":741},{"VI":742},"University of Birmingham College of Medical and Dental Sciences, School of Cancer Sciences, Edgbaston, UK",{"id":744,"sortIndex":216,"affiliation":745,"properties":752},"30ed58ab-07aa-4856-a2ff-8eedba2fd781",{"id":746,"createTime":747,"updateTime":747,"relativeEntities":748,"slug":19,"properties":749,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"4fcb8495-6f29-400b-8600-f8f91573ad36","2024-01-01T16:35:35.871+00:00",[],{"title":750},{"VI":751},"Department of Clinical Haematology, Nottingham University Hospitals, Nottingham, UK",{},{"title":754},{"VI":755},"Christopher P Fox",{"id":757,"sortIndex":216,"researcher":19,"roles":758,"affiliations":759,"properties":765},"bbe3a8f1-7ac6-4a5e-b502-a42fd53bcf73",[51],[760],{"id":19,"sortIndex":20,"affiliation":761,"properties":19},{"id":737,"createTime":738,"updateTime":738,"relativeEntities":762,"slug":19,"properties":763,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":764},{"VI":742},{"title":766},{"VI":767},"Claire Shannon-Lowe",{"id":769,"sortIndex":203,"researcher":19,"roles":770,"affiliations":771,"properties":777},"78227fc3-3370-48bb-a893-be4a2116757f",[51],[772],{"id":19,"sortIndex":20,"affiliation":773,"properties":19},{"id":737,"createTime":738,"updateTime":738,"relativeEntities":774,"slug":19,"properties":775,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":776},{"VI":742},{"title":778},{"VI":779},"Martin Rowe",{"url":729,"publisher":781,"properties":790},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":782,"slug":10,"properties":783,"entityType":17,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"subjectFields":787,"manageAffiliations":788,"indexDatabases":789,"url":19,"thumbnailPath":19,"statistic":19,"gsStatistic":19,"type":19,"analyzePriority":19},[],{"issn":784,"title":785,"url":786},{"VOID":13},{"EN":10},{"VOID":16},[],[],[],{"volume":791,"pages":792},{"VOID":327},{"VOID":793},"1-15","2011-09-07",{"id":796,"createTime":797,"updateTime":797,"relativeEntities":798,"slug":19,"properties":799,"entityType":43,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"primaryUrl":808,"fullTextUrl":19,"authors":809,"publicationType":240,"publisherRelationship":896,"citationCount":19,"citationInfo":19,"publishDate":909,"publishYear":257,"citationAnalyzeStatus":18,"lastCitationAnalyze":19,"indexDatabases":19,"openAccess":19,"references":19,"isForceReanalyzing":258},"29c388bc-d3ec-47de-bd36-741d470baddc","2023-12-31T10:01:15.981+00:00",[],{"references":800,"abstract":802,"title":804,"doi":806},{"VOID":801},"Melnick JL, Petrie BL, Dreesman GR, Burek J, McCollum CH, DeBakey ME: Cytomegalovirus antigen within human arterial smooth muscle cells. 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Circ Res. 2008, 102 (9): 1046-56. 10.1161\u002FCIRCRESAHA.108.174623.",{"EN":803},"Cytomegalovirus (CMV) infection has been associated with accelerated transplant vasculopathy. In this study, we assessed the effects of acute rat CMV (RCMV) infection on vessel remodeling in transplant vasculopathy, focusing on allograft morphology, inflammation and contribution of adventitial cells to intimal hyperplasia. Infrarenal aorta was locally infected with RCMV and transplanted from female F344 rats to male Lewis rats. Graft samples were collected 2 and 8 weeks after transplantation and analyzed for intimal hyperplasia, collagen degradation and inflammation. Transplantation of aorta followed by transplantation of RCMV infected and labeled isogenic adventitia were performed to study migration of adventitial cells towards the intima. Intimal hyperplasia was increased threefold in infected allografts. RCMV induced apoptosis in the media, expression of matrix metalloproteinase 2, and decreased collagen deposits. Macrophage infiltration was increased in the infected allografts and resulted in increased production of MCP-1. RCMV-infected macrophages were observed in the adventitia and intima. Cells derived from infected adventitia migrated towards the intima of the allograft. RCMV enhances infiltration of macrophages to the allografts, and thereby increases MCP-1 production and inflammation, followed by recruitment of adventitial cells to the intima and accelerated intimal hyperplasia.",{"EN":805},"RCMV increases intimal hyperplasia by inducing inflammation, MCP-1 expression and recruitment of adventitial cells to intima",{"VOID":807},"10.1186\u002F2042-4280-1-7","https:\u002F\u002Fherpesviridae.biomedcentral.com\u002Farticles\u002F10.1186\u002F2042-4280-1-7",[810,825,837,852,869,881],{"id":811,"sortIndex":20,"researcher":19,"roles":812,"affiliations":813,"properties":822},"f30e3a5c-3ead-4067-b153-20d1c2dabdf8",[51],[814],{"id":19,"sortIndex":20,"affiliation":815,"properties":19},{"id":816,"createTime":817,"updateTime":817,"relativeEntities":818,"slug":19,"properties":819,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"a55586f0-b2b4-47be-952b-e01355d26ca1","2023-12-31T10:01:16.044+00:00",[],{"title":820},{"VI":821},"Experimental Cardiovascular Research Unit, Department of Medicine, Solna, Karolinska Institutet, Stockholm, Sweden",{"title":823},{"VI":824},"Monika K Grudzinska",{"id":826,"sortIndex":119,"researcher":19,"roles":827,"affiliations":828,"properties":834},"fbdc1945-029a-45b3-9d09-cd82cfef1fc0",[51],[829],{"id":19,"sortIndex":20,"affiliation":830,"properties":19},{"id":816,"createTime":817,"updateTime":817,"relativeEntities":831,"slug":19,"properties":832,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":833},{"VI":821},{"title":835},{"VI":836},"Piotr Religa",{"id":838,"sortIndex":216,"researcher":19,"roles":839,"affiliations":840,"properties":849},"29bdd62a-2164-42c5-b159-695a3cc8efe0",[51],[841],{"id":19,"sortIndex":20,"affiliation":842,"properties":19},{"id":843,"createTime":844,"updateTime":844,"relativeEntities":845,"slug":19,"properties":846,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"8dc2f31e-ce96-4086-879e-952a3c146b7c","2023-12-31T10:01:16.005+00:00",[],{"title":847},{"VI":848},"Department of General, Vascular and Oncologic Surgery, Medical University of Warsaw, Warsaw, Poland",{"title":850},{"VI":851},"Krzysztof Bojakowski",{"id":853,"sortIndex":67,"researcher":19,"roles":854,"affiliations":855,"properties":866},"3300ebae-fd2d-4685-ba47-b0d51b92dc27",[51],[856],{"id":19,"sortIndex":20,"affiliation":857,"properties":19},{"id":858,"createTime":859,"updateTime":860,"relativeEntities":861,"slug":862,"properties":863,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"987d2d70-8cf1-42b2-a473-f44d34442285","2024-01-04T05:43:49.504+00:00","2024-11-25T12:37:03.422+00:00",[],"Maastricht-University-Medical-Center-Maastricht-The-Netherlands",{"title":864},{"VI":865},"Maastricht University Medical Center, Maastricht, The Netherlands",{"title":867},{"VI":868},"Frank Stassen",{"id":870,"sortIndex":229,"researcher":19,"roles":871,"affiliations":872,"properties":878},"97b5da3c-a0d6-4a87-81f0-35147efc3adc",[51],[873],{"id":19,"sortIndex":20,"affiliation":874,"properties":19},{"id":816,"createTime":817,"updateTime":817,"relativeEntities":875,"slug":19,"properties":876,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},[],{"title":877},{"VI":821},{"title":879},{"VI":880},"Cecilia Söderberg-Nauclér",{"id":882,"sortIndex":203,"researcher":19,"roles":883,"affiliations":884,"properties":893},"a26475fa-f1cb-4f3a-9c28-622aaf9d7929",[51],[885],{"id":19,"sortIndex":20,"affiliation":886,"properties":19},{"id":887,"createTime":888,"updateTime":888,"relativeEntities":889,"slug":19,"properties":890,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"fd6c7559-d072-45b9-8bd3-235bc607d63c","2023-12-31T10:01:16.017+00:00",[],{"title":891},{"VI":892},"Department of General Biochemistry and Nutrition, Medical University of Warsaw, Warsaw, Poland",{"title":894},{"VI":895},"Joanna Soin",{"url":808,"publisher":897,"properties":906},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":898,"slug":10,"properties":899,"entityType":17,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"subjectFields":903,"manageAffiliations":904,"indexDatabases":905,"url":19,"thumbnailPath":19,"statistic":19,"gsStatistic":19,"type":19,"analyzePriority":19},[],{"issn":900,"title":901,"url":902},{"VOID":13},{"EN":10},{"VOID":16},[],[],[],{"volume":907,"pages":908},{"VOID":253},{"VOID":329},"2010-12-23",{"id":911,"createTime":912,"updateTime":913,"relativeEntities":914,"slug":915,"properties":916,"entityType":43,"verifyStatus":44,"verifyTime":913,"verifyNote":45,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20,"primaryUrl":925,"fullTextUrl":19,"authors":926,"publicationType":240,"publisherRelationship":1041,"citationCount":19,"citationInfo":19,"publishDate":1055,"publishYear":331,"citationAnalyzeStatus":18,"lastCitationAnalyze":19,"indexDatabases":19,"openAccess":19,"references":19,"isForceReanalyzing":258},"a0495569-7cd5-4da5-b15d-71e0c36bb5bf","2024-01-18T00:50:22.114+00:00","2025-02-20T09:48:41.523+00:00",[],"Circulating-herpes-simplex-type-1-HSV-1-specific-CD8-T-cells-do-not-access-HSV-1-latently-infected-trigeminal-ganglia",{"references":917,"abstract":919,"title":921,"doi":923},{"VOID":918},"Arduino PG, Porter SR: Herpes Simplex Virus Type 1 infection: overview on relevant clinico-pathological features. 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Invest Ophthalmol Vis Sci. 2006, 47 (8): 3400-9. 10.1167\u002Fiovs.05-0898.\nGao P, et al: The unique target specificity of a nonpeptide chemokine receptor antagonist: selective blockade of two Th1 chemokine receptors CCR5 and CXCR3. J Leukoc Biol. 2003, 73 (2): 273-80. 10.1189\u002Fjlb.0602269.\nFrank GM, et al: A novel p40-independent function of IL-12p35 is required for progression and maintenance of herpes stromal keratitis. Invest Ophthalmol Vis Sci. 51 (7): 3591-8. 10.1167\u002Fiovs.09-4368.\nBelz GT, et al: Minimal activation of memory CD8+ T cell by tissue-derived dendritic cells favors the stimulation of naive CD8+ T cells. Nat Immunol. 2007, 8 (10): 1060-6. 10.1038\u002Fni1505.\nBaba M, et al: A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-HIV-1 activity. Proc Natl Acad Sci USA. 1999, 96 (10): 5698-703. 10.1073\u002Fpnas.96.10.5698.\nWakim LM, et al: Dendritic cell-induced memory T cell activation in nonlymphoid tissues. Science. 2008, 319 (5860): 198-202. 10.1126\u002Fscience.1151869.\nHoshino Y, et al: Rates of reactivation of latent herpes simplex virus from mouse trigeminal ganglia ex vivo correlate directly with viral load and inversely with number of infiltrating CD8+ T cells. J Virol. 2007, 81 (15): 8157-64. 10.1128\u002FJVI.00474-07.\nDerfuss T, et al: The presence of lytic HSV-1 transcripts and clonally expanded T cells with a memory effector phenotype in human sensory ganglia. Ann N Y Acad Sci. 2009, 1164: 300-4. 10.1111\u002Fj.1749-6632.2009.03871.x.\nWickham S, et al: Chemokine receptor deficiency is associated with increased chemokine expression in the peripheral and central nervous systems and increased resistance to herpetic encephalitis. J Neuroimmunol. 2005, 162 (1-2): 51-9. 10.1016\u002Fj.jneuroim.2005.01.001.\nCook WJ, et al: Persistent expression of chemokine and chemokine receptor RNAs at primary and latent sites of herpes simplex virus 1 infection. Virol J. 2004, 1: 5-10.1186\u002F1743-422X-1-5.\nWakim LM, Woodward-Davis A, Bevan MJ: Inaugural Article: Memory T cells persisting within the brain after local infection show functional adaptations to their tissue of residence. Proc Natl Acad Sci USA.\nTait AS, Butts CL, Sternberg EM: The role of glucocorticoids and progestins in inflammatory, autoimmune, and infectious disease. J Leukoc Biol. 2008, 84 (4): 924-31. 10.1189\u002Fjlb.0208104.\nFrank GM, et al: Early CD4(+) T cell help prevents partial CD8(+) T cell exhaustion and promotes maintenance of Herpes Simplex Virus 1 latency. J Immunol. 184 (1): 277-86. 10.4049\u002Fjimmunol.0902373.",{"EN":920},"Therapeutic vaccines can be designed to enhance existing T cell memory populations for increased protection against re-infection. In the case of herpes simplex virus type 1, recurrent disease results from reactivation of latent virus in sensory ganglia, which is controlled in part by a ganglia-resident HSV-specific memory CD8+ T cell population. Thus, an important goal of a therapeutic HSV-1 vaccine would be to enhance this population. HSV-1-infected mice were treated with TAK-779 to block CCR5- and CXCR3-mediated CD8+ T cell migration during both acute and latent infections. Additionally, HSV-1-specific CD8+ T cells were transferred into HSV-1 latently infected mice to mimic the effect of a therapeutic vaccine, and their migration into trigeminal ganglia (TG) was traced during steady-state latency, or during recovery of the TG-resident memory CD8+ T cell population following stress-, and corticosterone-induced depletion and HSV-1 reactivation from latency. Bromodeoxy uridine (BrdU) incorporation measured cell proliferation in vivo. TAK-779 treatment during acute HSV-1 infection reduced the number of infiltrating CD8+ T cells but did not alter the number of viral genome copies. TAK-779 treatment during HSV latency did not affect the size of the TG-resident memory CD8+ T cell population. Transferred HSV-specific CD8+ T cells failed to access latently infected TG during steady-state latency, or during recovery of the TG resident HSV-specific CD8+ T cell population following exposure of latently infected mice to stress and corticosterone. Recovery of the HSV-specific CD8+ T cell population after stress and corticosterone treatment occurred with homeostatic levels of cell division and did not require CD4+ T cell help. Our findings are consistent with the notion that the CD8+ T cells in latently infected TG are a tissue-resident memory (Trm) population that is maintained without replenishment from the periphery, and that when this population is disrupted, it recovers without proliferation or detectable recruitment of HSV-specific CD8+ T cells from the blood. The compartmentalization of the HSV-specific CD8+ memory T cell population in latently infected TG will complicate the design of therapeutic vaccines.",{"EN":922},"Circulating herpes simplex type 1 (HSV-1)-specific CD8+T cells do not access HSV-1 latently infected trigeminal ganglia",{"VOID":924},"10.1186\u002F2042-4280-2-5","https:\u002F\u002Fherpesviridae.biomedcentral.com\u002Farticles\u002F10.1186\u002F2042-4280-2-5",[927,952,964,981,993,1010],{"id":928,"sortIndex":216,"researcher":19,"roles":929,"affiliations":930,"properties":949},"237a0253-07cf-4dae-84ef-a1383b2fa4d0",[51],[931,939],{"id":19,"sortIndex":20,"affiliation":932,"properties":19},{"id":933,"createTime":934,"updateTime":934,"relativeEntities":935,"slug":19,"properties":936,"entityType":61,"verifyStatus":18,"verifyTime":19,"verifyNote":19,"syncStatus":18,"languages":19,"translateLanguages":19,"viewCount":20},"9b61962d-c8fc-4c80-b7c3-5f4d6d342de5","2024-01-12T16:07:21.997+00:00",[],{"title":937},{"VI":938},"Department of 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