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We previously reported an abundant accumulation of small subgenomic flaviviral RNA (sfRNA) which is collinear with the highly conserved regions of the 3'-UTR in JEV-infected cells. However, function of the sfRNA in JEV life cycle remains unknown. Northern blot and real-time RT-PCR analyses indicated that the sfRNA becomes apparent at the time point at which minus-strand RNA (antigenome) reaches a plateau suggesting a role for sfRNA in the regulation of antigenome synthesis. Transfection of minus-sense sfRNA into JEV-infected cells, in order to counter the effects of plus-sense sfRNA, resulted in higher levels of antigenome suggesting that the presence of the sfRNA inhibits antigenome synthesis. Trans-acting effect of sfRNA on JEV translation was studied using a reporter mRNA containing the luciferase gene fused to partial coding regions of JEV and flanked by the respective JEV UTRs. In vivo and in vitro translation revealed that sfRNA inhibited JEV translation. Our results indicate that sfRNA modulates viral translation and replication in trans.",{"EN":137},"Small noncoding RNA modulates japanese encephalitis virus replication and translation in trans",{"VOID":139},"Endy TP, Nisalak A: Japanese encephalitis virus: ecology and epidemiology. Curr Top Microbiol Immunol 2002, 267: 11-48. 10.1007\u002F978-3-642-59403-8_2\nErlanger TE, Weiss S, Keiser J, Utzinger J, Wiedenmayer K: Past, present, and future of Japanese encephalitis. Emerg Infect Dis 2009, 15: 1-7. 10.3201\u002Feid1501.080311\nLindenbach BD, Thiel H-J, Rice CM: Flaviviridae: The Viruses and Their Replication. In Fields Virology. Volume 1. 5th edition. Edited by: Knipe DM, Howley PM. Philadephia, PA.: Lippincott William & Wilkins; 2007:1101-1152.\nChu PW, Westaway EG: Replication strategy of Kunjin virus: evidence for recycling role of replicative form RNA as template in semiconservative and asymmetric replication. Virology 1985, 140: 68-79. 10.1016\u002F0042-6822(85)90446-5\nCleaves GR, Ryan TE, Schlesinger RW: Identification and characterization of type 2 dengue virus replicative intermediate and replicative form RNAs. Virology 1981, 111: 73-83. 10.1016\u002F0042-6822(81)90654-1\nTakegami T, Hotta S: Synthesis and localization of Japanese encephalitis virus RNAs in the infected cells. Microbiol Immunol 1990, 34: 849-857.\nUchil PD, Satchidanandam V: Characterization of RNA synthesis, replication mechanism, and in vitro RNA-dependent RNA polymerase activity of Japanese encephalitis virus. Virology 2003, 307: 358-371. 10.1016\u002FS0042-6822(02)00130-7\nLin KC, Chang HL, Chang RY: Accumulation of a 3'-terminal genome fragment in Japanese encephalitis virus-infected mammalian and mosquito cells. J Virol 2004, 78: 5133-5138. 10.1128\u002FJVI.78.10.5133-5138.2004\nFunk A, Truong K, Nagasaki T, Torres S, Floden N, Balmori Melian E, Edmonds J, Dong H, Shi PY, Khromykh AA: RNA structures required for production of subgenomic flavivirus RNA. J Virol 2010, 84: 11407-11417. 10.1128\u002FJVI.01159-10\nSilva PA, Pereira CF, Dalebout TJ, Spaan WJ, Bredenbeek PJ: An RNA pseudoknot is required for production of yellow fever virus subgenomic RNA by the host nuclease XRN1. J Virol 2010, 84: 11395-11406. 10.1128\u002FJVI.01047-10\nPijlman GP, Funk A, Kondratieva N, Leung J, Torres S, van der Aa L, Liu WJ, Palmenberg AC, Shi PY, Hall RA, Khromykh AA: A highly structured, nuclease-resistant, noncoding RNA produced by flaviviruses is required for pathogenicity. Cell Host Microbe 2008, 4: 579-591. 10.1016\u002Fj.chom.2008.10.007\nAlvarez DE, De Lella Ezcurra AL, Fucito S, Gamarnik AV: Role of RNA structures present at the 3'UTR of dengue virus on translation, RNA synthesis, and viral replication. Virology 2005, 339: 200-212. 10.1016\u002Fj.virol.2005.06.009\nHolden KL, Harris E: Enhancement of dengue virus translation: role of the 3' untranslated region and the terminal 3' stem-loop domain. Virology 2004, 329: 119-133. 10.1016\u002Fj.virol.2004.08.004\nYoo JS, Kim CM, Kim JH, Kim JY, Oh JW: Inhibition of Japanese encephalitis virus replication by peptide nucleic acids targeting cis-acting elements on the plus- and minus-strands of viral RNA. Antiviral Res 2009, 82: 122-133. 10.1016\u002Fj.antiviral.2009.02.187\nPolacek C, Friebe P, Harris E: Poly(A)-binding protein binds to the non-polyadenylated 3' untranslated region of dengue virus and modulates translation efficiency. J Gen Virol 2009, 90: 687-692. 10.1099\u002Fvir.0.007021-0\nTilgner M, Shi PY: Structure and function of the 3' terminal six nucleotides of the West Nile virus genome in viral replication. J Virol 2004, 78: 8159-8171. 10.1128\u002FJVI.78.15.8159-8171.2004\nKhromykh AA, Westaway EG: RNA binding properties of core protein of the flavivirus Kunjin. Arch Virol 1996, 141: 685-699. 10.1007\u002FBF01718326\nHahn CS, Hahn YS, Rice CM, Lee E, Dalgarno L, Strauss EG, Strauss JH: Conserved elements in the 3' untranslated region of flavivirus RNAs and potential cyclization sequences. J Mol Biol 1987, 198: 33-41. 10.1016\u002F0022-2836(87)90455-4\nAlvarez DE, Filomatori CV, Gamarnik AV: Functional analysis of dengue virus cyclization sequences located at the 5' and 3'UTRs. Virology 2008, 375: 223-235. 10.1016\u002Fj.virol.2008.01.014\nFriebe P, Harris E: Interplay of RNA elements in the dengue virus 5' and 3' ends required for viral RNA replication. J Virol 2010, 84: 6103-6118. 10.1128\u002FJVI.02042-09\nSuzuki R, Fayzulin R, Frolov I, Mason PW: Identification of mutated cyclization sequences that permit efficient replication of West Nile virus genomes: use in safer propagation of a novel vaccine candidate. J Virol 2008, 82: 6942-6951. 10.1128\u002FJVI.00662-08\nVillordo SM, Gamarnik AV: Genome cyclization as strategy for flavivirus RNA replication. Virus Res 2009, 139: 230-239. 10.1016\u002Fj.virusres.2008.07.016\nZhang B, Dong H, Stein DA, Iversen PL, Shi PY: West Nile virus genome cyclization and RNA replication require two pairs of long-distance RNA interactions. Virology 2008, 373: 1-13. 10.1016\u002Fj.virol.2008.01.016\nFriebe P, Harris E: Interplay of RNA elements in the dengue virus 5' and 3' ends required for viral RNA replication. J Virol 2010, 84: 6103-6118. 10.1128\u002FJVI.02042-09\nYun SI, Choi YJ, Song BH, Lee YM: 3' cis-acting elements that contribute to the competence and efficiency of Japanese encephalitis virus genome replication: functional importance of sequence duplications, deletions, and substitutions. J Virol 2009, 83: 7909-7930. 10.1128\u002FJVI.02541-08\nBlackwell JL, Brinton MA: BHK cell proteins that bind to the 3' stem-loop structure of the West Nile virus genome RNA. J Virol 1995, 69: 5650-5658.\nBlackwell JL, Brinton MA: Translation elongation factor-1 alpha interacts with the 3' stem-loop region of West Nile virus genomic RNA. J Virol 1997, 71: 6433-6444.\nDavis WG, Blackwell JL, Shi PY, Brinton MA: Interaction between the cellular protein eEF1A and the 3'-terminal stem-loop of West Nile virus genomic RNA facilitates viral minus-strand RNA synthesis. J Virol 2007, 81: 10172-10187. 10.1128\u002FJVI.00531-07\nEmara MM, Liu H, Davis WG, Brinton MA: Mutation of mapped TIA-1\u002FTIAR binding sites in the 3' terminal stem-loop of West Nile virus minus-strand RNA in an infectious clone negatively affects genomic RNA amplification. J Virol 2008, 82: 10657-10670. 10.1128\u002FJVI.00991-08\nYocupicio-Monroy M, Padmanabhan R, Medina F, del Angel RM: Mosquito La protein binds to the 3' untranslated region of the positive and negative polarity dengue virus RNAs and relocates to the cytoplasm of infected cells. Virology 2007, 357: 29-40. 10.1016\u002Fj.virol.2006.07.042\nDe Nova-Ocampo M, Villegas-Sepulveda N, del Angel RM: Translation elongation factor-1alpha, La, and PTB interact with the 3' untranslated region of dengue 4 virus RNA. Virology 2002, 295: 337-347. 10.1006\u002Fviro.2002.1407\nParanjape SM, Harris E: Y box-binding protein-1 binds to the dengue virus 3'-untranslated region and mediates antiviral effects. J Biol Chem 2007, 282: 30497-30508. 10.1074\u002Fjbc.M705755200\nWei Y, Qin C, Jiang T, Li X, Zhao H, Liu Z, Deng Y, Liu R, Chen S, Yu M, Qin E: Translational regulation by the 3' untranslated region of the dengue type 2 virus genome. Am J Trop Med Hyg 2009, 81: 817-824. 10.4269\u002Fajtmh.2009.08-0595\nRakotondrafara AM, Polacek C, Harris E, Miller WA: Oscillating kissing stem-loop interactions mediate 5' scanning-dependent translation by a viral 3'-cap-independent translation element. RNA 2006, 12: 1893-1906. 10.1261\u002Frna.115606\nChiu WW, Kinney RM, Dreher TW: Control of translation by the 5'- and 3'-terminal regions of the dengue virus genome. J Virol 2005, 79: 8303-8315. 10.1128\u002FJVI.79.13.8303-8315.2005\nGomila RC, Martin GW, Gehrke L: NF90 binds the dengue virus RNA 3' terminus and is a positive regulator of dengue virus replication. PLoS One 2011, 6: e16687. 10.1371\u002Fjournal.pone.0016687\nChen CJ, Kuo MD, Chien LJ, Hsu SL, Wang YM, Lin JH: RNA-protein interactions: involvement of NS3, NS5, and 3' noncoding regions of Japanese encephalitis virus genomic RNA. J Virol 1997, 71: 3466-3473.\nTa M, Vrati S: Mov34 protein from mouse brain interacts with the 3' noncoding region of Japanese encephalitis virus. J Virol 2000, 74: 5108-5115. 10.1128\u002FJVI.74.11.5108-5115.2000\nVashist S, Anantpadma M, Sharma H, Vrati S: La protein binds the predicted loop structures in the 3' non-coding region of Japanese encephalitis virus genome: role in virus replication. J Gen Virol 2009, 90: 1343-1352. 10.1099\u002Fvir.0.010850-0\nYang SH, Liu ML, Tien CF, Chou SJ, Chang RY: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interaction with 3' ends of Japanese encephalitis virus RNA and colocalization with the viral NS5 protein. J Biomed Sci 2009, 16: 40. 10.1186\u002F1423-0127-16-40\nUchil PD, Kumar AV, Satchidanandam V: Nuclear localization of flavivirus RNA synthesis in infected cells. J Virol 2006, 80: 5451-5464. 10.1128\u002FJVI.01982-05\nTakegami T, Hotta S: In vitro synthesis of Japanese encephalitis virus (JEV) RNA: membrane and nuclear fractions of JEV-infected cells possess high levels of virus-specific RNA polymerase activity. Virus Res 1989, 13: 337-350. 10.1016\u002F0168-1702(89)90078-6\nMori Y, Okabayashi T, Yamashita T, Zhao Z, Wakita T, Yasui K, Hasebe F, Tadano M, Konishi E, Moriishi K, Matsuura Y: Nuclear localization of Japanese encephalitis virus core protein enhances viral replication. J Virol 2005, 79: 3448-3458. 10.1128\u002FJVI.79.6.3448-3458.2005\nZhang G, Zhang J, Simon AE: Repression and derepression of minus-strand synthesis in a plus-strand RNA virus replicon. J Virol 2004, 78: 7619-7633. 10.1128\u002FJVI.78.14.7619-7633.2004\nPogany J, Fabian MR, White KA, Nagy PD: A replication silencer element in a plus-strand RNA virus. Embo J 2003, 22: 5602-5611. 10.1093\u002Femboj\u002Fcdg523\nSivakumaran K, Kim CH, Tayon R, Kao CC: RNA sequence and secondary structural determinants in a minimal viral promoter that directs replicase recognition and initiation of genomic plus-strand RNA synthesis. J Mol Biol 1999, 294: 667-682. 10.1006\u002Fjmbi.1999.3297\nFrolov I, Hardy R, Rice CM: Cis-acting RNA elements at the 5' end of Sindbis virus genome RNA regulate minus- and plus-strand RNA synthesis. Rna 2001, 7: 1638-1651. 10.1017\u002FS135583820101010X\nSatyanarayana T, Gowda S, Ayllon MA, Albiach-Marti MR, Rabindran S, Dawson WO: The p23 protein of citrus tristeza virus controls asymmetrical RNA accumulation. J Virol 2002, 76: 473-483. 10.1128\u002FJVI.76.2.473-483.2002\nWang RY, Nagy PD: Tomato bushy stunt virus co-opts the RNA-binding function of a host metabolic enzyme for viral genomic RNA synthesis. Cell Host Microbe 2008, 3: 178-187. 10.1016\u002Fj.chom.2008.02.005\nWang X, Ahlquist P: Filling a GAP(DH) in asymmetric viral RNA synthesis. Cell Host Microbe 2008, 3: 124-125. 10.1016\u002Fj.chom.2008.02.012\nFilomatori CV, Lodeiro MF, Alvarez DE, Samsa MM, Pietrasanta L, Gamarnik AV: A 5' RNA element promotes dengue virus RNA synthesis on a circular genome. Genes Dev 2006, 20: 2238-2249. 10.1101\u002Fgad.1444206\nVillordo SM, Alvarez DE, Gamarnik AV: A balance between circular and linear forms of the dengue virus genome is crucial for viral replication. Rna 2010, 16: 2325-2335. 10.1261\u002Frna.2120410\nChen LK, Lin YL, Liao CL, Lin CG, Huang YL, Yeh CT, Lai SC, Jan JT, Chin C: Generation and characterization of organ-tropism mutants of Japanese encephalitis virus in vivo and in vitro. Virology 1996, 223: 79-88. 10.1006\u002Fviro.1996.0457\nWang WK, Sung TL, Tsai YC, Kao CL, Chang SM, King CC: Detection of dengue virus replication in peripheral blood mononuclear cells from dengue virus type 2-infected patients by a reverse transcription-real-time PCR assay. J Clin Microbiol 2002, 40: 4472-4478. 10.1128\u002FJCM.40.12.4472-4478.2002",{"VOID":141},"10.1186\u002F1743-422X-8-492","PUBLICATION","VERIFIED","2024-09-05T08:19:02.193+00:00","Auto Verify","https:\u002F\u002Fvirologyj.biomedcentral.com\u002Farticles\u002F10.1186\u002F1743-422X-8-492",[148,164,178,191,205,219],{"id":149,"sortIndex":21,"researcher":20,"roles":150,"affiliations":152,"properties":161},"2272efe8-9c06-4094-96ce-8a6ee4deb60b",[151],"AUTHOR",[153],{"id":154,"sortIndex":21,"affiliation":155,"properties":20},"1ad3fb20-fdf5-4ba1-a4b3-416df9226293",{"id":154,"createTime":20,"updateTime":20,"relativeEntities":156,"slug":20,"properties":157,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":160,"statistic":20},[],{"title":158},{"VI":159},"Department of Life Science and Institute of Biotechnology, National Dong Hwa University, Taiwan",[],{"title":162},{"VI":163},"Yi-Hsin 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               \u003Cjats:title>Background\u003C\u002Fjats:title>\n                \u003Cjats:p>There are many studies on the relationship between vitamin D and coronavirus disease 2019 (COVID-19), while the results are matters of debate and the mechanisms remain unknown. The present study was performed to assess the impact of serum 25-hydroxyvitamin D [25(OH)D] levels on the severity of disease in hospitalized COVID-19 patients and identify potential mechanisms of 25(OH)D alterations.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Methods\u003C\u002Fjats:title>\n                \u003Cjats:p>A total of 399 hospitalized COVID-19 patients were recruited from three centers between December 19, 2022, and February 1, 2023. Medical history, laboratory examination, and radiologic data were retrospectively collected. The patients were divided into four groups based on disease severity. Serum 25(OH)D levels in the patients were determined by the electrochemiluminescence method and cytokines were detected by flow cytometry. The relationship between serum 25(OH)D status and the severity of COVID-19, and the correlation between 25(OH)D levels and cytokines in COVID-19 patients were assessed.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Results\u003C\u002Fjats:title>\n                \u003Cjats:p>Levels of 25(OH)D were significantly lower in the deceased group than in the other three groups (\u003Cjats:italic>P\u003C\u002Fjats:italic> < 0.05), and lower in the critical group than in the general group (\u003Cjats:italic>P\u003C\u002Fjats:italic> < 0.05). There were no significant differences in the 25(OH)D levels between the general and severe groups (\u003Cjats:italic>P\u003C\u002Fjats:italic> > 0.05). The levels of 25(OH)D (odds ratio = 0.986, 95% confidence interval: 0.973–0.998, \u003Cjats:italic>P\u003C\u002Fjats:italic> = 0.024) and IL-5 (odds ratio = 1.239, 95% confidence interval: 1.104–1.391, \u003Cjats:italic>P\u003C\u002Fjats:italic> = 0.04) were independent risk factors for the severity of COVID-19 disease upon admission. Serum 25(OH)D levels were able to predict the mortality of patients with COVID-19, and the predictive value was even higher when combined with IL-5 levels and eosinophil (Eos) count. Circulating 25(OH)D status correlated negatively with the expression of IL-5 (r=-0.262, \u003Cjats:italic>P\u003C\u002Fjats:italic> < 0.001) and was positively linked with CD8\u003Cjats:sup>+\u003C\u002Fjats:sup> T cell counts (r=-0.121, \u003Cjats:italic>P\u003C\u002Fjats:italic> < 0.05) in patients with COVID-19.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Conclusions\u003C\u002Fjats:title>\n                \u003Cjats:p>This study found that the serum 25(OH)D status combined with IL-5 levels and Eos counts could be identified as a predictive factor for recognizing the risk of COVID-19 mortality. The serum 25(OH)D status in COVID-19 patients correlated negatively with the expression of IL-5. The potential mechanism for this relationship is worth further exploration.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>",{"EN":302},"Vitamin D status in hospitalized COVID‑19 patients is associated with disease severity and IL-5 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Is vitamin D deficiency a risk factor for COVID-19 in children? Pediatr Pulmonol. 2020;55(12):3595–601. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fppul.25106.",{"doi":576},"10.1002\u002Fppul.25106",{"id":20,"text":578,"url":20,"identifiers":579},"Sabico S, Enani MA, Sheshah E, et al. Effects of a 2-Week 5000 IU versus 1000 IU vitamin D3 supplementation on recovery of symptoms in patients with mild to moderate Covid-19: a Randomized Clinical Trial. Nutrients. 2021;13(7). https:\u002F\u002Fdoi.org\u002F10.3390\u002Fnu13072170.",{"doi":580},"10.3390\u002Fnu13072170",{"id":20,"text":582,"url":20,"identifiers":583},"Ilie PC, Stefanescu S, Smith L. The role of vitamin D in the prevention of coronavirus disease 2019 infection and mortality. Aging Clin Exp Res. 2020;32(7):1195–8. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs40520-020-01570-8.",{"doi":584},"10.1007\u002Fs40520-020-01570-8",{"id":20,"text":586,"url":20,"identifiers":587},"Alpcan A, Tursun S, Kandur Y. 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Nutrients. 2020;12(12). https:\u002F\u002Fdoi.org\u002F10.3390\u002Fnu12123799.",{"doi":620},"10.3390\u002Fnu12123799",{"id":20,"text":622,"url":20,"identifiers":623},"Gounari E, Chatzizisi O, Diza-Mataftsi E, et al. Potential prognostic value of intracellular cytokine detection by flow cytometry in pulmonary sarcoidosis. J Interferon Cytokine Res. 2013;33(5):261–9. https:\u002F\u002Fdoi.org\u002F10.1089\u002Fjir.2012.0022.",{"doi":624},"10.1089\u002Fjir.2012.0022",{"id":20,"text":626,"url":20,"identifiers":627},"Popovska Jovicic B, Rakovic I, Gavrilovic J, et al. Vitamin D, Albumin, and D-Dimer as significant prognostic markers in early hospitalization in patients with COVID-19. J Clin Med. 2023;12(8). https:\u002F\u002Fdoi.org\u002F10.3390\u002Fjcm12082825.",{"doi":628},"10.3390\u002Fjcm12082825",{"id":20,"text":630,"url":20,"identifiers":631},"Protas VV, Pogossyan GP, Li KG, et al. Plasma 25-Hydroxyvitamin D level and VDR gene single nucleotide polymorphism rs2228570 influence on COVID-19 susceptibility among the Kazakh ethnic Group-A pilot study. Nutrients. 2023;15(7). https:\u002F\u002Fdoi.org\u002F10.3390\u002Fnu15071781.",{"doi":632},"10.3390\u002Fnu15071781",{"id":20,"text":634,"url":20,"identifiers":635},"Slomski A. Vitamin D supplements don’t reduce COVID-19 risk. JAMA. 2022;328(16):1581doi. https:\u002F\u002Fdoi.org\u002F10.1001\u002Fjama.2022.15486.",{"doi":636},"10.1001\u002Fjama.2022.15486",{"id":20,"text":638,"url":20,"identifiers":639},"Hernandez JL, Nan D, Fernandez-Ayala M, et al. Vitamin D status in hospitalized patients with SARS-CoV-2 infection. J Clin Endocrinol Metab. 2021;106(3):e1343–53. https:\u002F\u002Fdoi.org\u002F10.1210\u002Fclinem\u002Fdgaa733.",{"doi":640},"10.1210\u002Fclinem\u002Fdgaa733",{"id":20,"text":642,"url":20,"identifiers":643},"Mandal AKJ, Baktash V, Hosack T, et al. Vitamin D status may indeed be a prognosticator for morbidity and mortality in patients with COVID-19. J Med Virol. 2021;93(3):1225doi. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fjmv.26569.",{"doi":644},"10.1002\u002Fjmv.26569",{"id":20,"text":646,"url":20,"identifiers":647},"Azkur AK, Akdis M, Azkur D, et al. Immune response to SARS-CoV-2 and mechanisms of immunopathological changes in COVID-19. Allergy. 2020;75(7):1564–81. https:\u002F\u002Fdoi.org\u002F10.1111\u002Fall.14364.",{"doi":648},"10.1111\u002Fall.14364",{"id":20,"text":650,"url":20,"identifiers":651},"Favaloro EJ, Lippi G. Recommendations for Minimal Laboratory Testing Panels in patients with COVID-19: potential for prognostic monitoring. Semin Thromb Hemost. 2020;46(3):379–82. https:\u002F\u002Fdoi.org\u002F10.1055\u002Fs-0040-1709498.",{"doi":652},"10.1055\u002Fs-0040-1709498",{"id":20,"text":654,"url":20,"identifiers":655},"Chen T, Wu D, Chen H, et al. Clinical characteristics of 113 deceased patients with coronavirus disease 2019: retrospective study. BMJ. 2020;368:m1091. https:\u002F\u002Fdoi.org\u002F10.1136\u002Fbmj.m1091.",{"doi":656},"10.1136\u002Fbmj.m1091",{"id":20,"text":658,"url":20,"identifiers":659},"Pala D, Pistis M. Anti-IL5 drugs in COVID-19 patients: role of Eosinophils in SARS-CoV-2-Induced Immunopathology. Front Pharmacol. 2021;12:622554. https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffphar.2021.622554.",{"doi":660},"10.3389\u002Ffphar.2021.622554",{"id":20,"text":662,"url":20,"identifiers":663},"Schoenmakers I, Fraser WD, Forbes A. Vitamin D and acute and severe illness - a mechanistic and pharmacokinetic perspective. Nutr Res Rev. 2023;36(1):23–38. https:\u002F\u002Fdoi.org\u002F10.1017\u002FS0954422421000251.",{"doi":664},"10.1017\u002FS0954422421000251",{"id":20,"text":666,"url":20,"identifiers":667},"Liu Y, Zhang C, Huang F, et al. Elevated plasma levels of selective cytokines in COVID-19 patients reflect viral load and lung injury. Natl Sci Rev. 2020;7(6):1003–11. https:\u002F\u002Fdoi.org\u002F10.1093\u002Fnsr\u002Fnwaa037.",{"doi":668},"10.1093\u002Fnsr\u002Fnwaa037",{"id":20,"text":670,"url":20,"identifiers":671},"Singh SK, Jain R, Singh S. Vitamin D deficiency in patients with diabetes and COVID- 19 infection. Diabetes Metab Syndr. 2020;14(5):1033–5. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.dsx.2020.06.071.",{"doi":672},"10.1016\u002Fj.dsx.2020.06.071",{"id":20,"text":674,"url":20,"identifiers":675},"Han Y, Zhang H, Mu S, et al. Lactate dehydrogenase, an independent risk factor of severe COVID-19 patients: a retrospective and observational study. Aging. 2020;12(12):11245–58. https:\u002F\u002Fdoi.org\u002F10.18632\u002Faging.103372.",{"doi":676},"10.18632\u002Faging.103372",{"id":20,"text":678,"url":20,"identifiers":679},"Sun Y, Dong Y, Wang L, et al. Characteristics and prognostic factors of disease severity in patients with COVID-19: the Beijing experience. J Autoimmun. 2020;112:102473. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jaut.2020.102473.",{"doi":680},"10.1016\u002Fj.jaut.2020.102473",{"id":20,"text":682,"url":20,"identifiers":683},"Chen R, Sang L, Jiang M, et al. Longitudinal hematologic and immunologic variations associated with the progression of COVID-19 patients in China. J Allergy Clin Immunol. 2020;146(1):89–100. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jaci.2020.05.003.",{"doi":684},"10.1016\u002Fj.jaci.2020.05.003",{"id":20,"text":686,"url":20,"identifiers":687},"Bilezikian JP, Bikle D, Hewison M, et al. MECHANISMS IN ENDOCRINOLOGY: vitamin D and COVID-19. Eur J Endocrinol. 2020;183(5):R133–47. https:\u002F\u002Fdoi.org\u002F10.1530\u002FEJE-20-0665.",{"doi":688},"10.1530\u002FEJE-20-0665",{"id":20,"text":690,"url":20,"identifiers":691},"Chiodini I, Gatti D, Soranna D, et al. Vitamin D status and SARS-CoV-2 infection and COVID-19 clinical outcomes. Front Public Health. 2021;9:736665. https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffpubh.2021.736665.",{"doi":692},"10.3389\u002Ffpubh.2021.736665",{"id":20,"text":694,"url":20,"identifiers":695},"Poddighe D, Kovzel E. Impact of anti-type 2 inflammation biologic therapy on COVID-19 clinical course and outcome. J Inflamm Res. 2021;14:6845–53. https:\u002F\u002Fdoi.org\u002F10.2147\u002FJIR.S345665.",{"doi":696},"10.2147\u002FJIR.S345665",{"id":20,"text":698,"url":20,"identifiers":699},"Zhou Y, Qiu Y, Bao W, et al. Evaluating the effects of vitamin D level on airway obstruction in two asthma endotypes in humans and in two mouse models with different intake of vitamin D during early-life. Front Immunol. 2023;14:1107031. https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffimmu.2023.1107031.",{"doi":700},"10.3389\u002Ffimmu.2023.1107031",{"id":20,"text":702,"url":20,"identifiers":703},"Zhou Y, Xue Y, Bao A, et al. Effect of vitamin D Deficiency and Supplementation in Lactation and Early Life on allergic airway inflammation and the expression of Autophagy-Related genes in an Ovalbumin Mouse Model. J Inflamm Res. 2021;14:4125–41. https:\u002F\u002Fdoi.org\u002F10.2147\u002FJIR.S321642.",{"doi":704},"10.2147\u002FJIR.S321642",{"id":706,"createTime":707,"updateTime":708,"relativeEntities":709,"slug":710,"properties":711,"entityType":142,"verifyStatus":143,"verifyTime":721,"verifyNote":145,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":722,"fullTextUrl":20,"authors":723,"publicationType":233,"publisherRelationship":834,"citationCount":20,"citationInfo":20,"publishDate":885,"publishYear":886,"citationAnalyzeStatus":533,"lastCitationAnalyze":887,"indexDatabases":888,"openAccess":20,"references":20,"isForceReanalyzing":289},"c31ae379-cf1d-4d6a-8171-f50afafa17b4","2023-12-07T22:32:08.478+00:00","2026-08-14T18:20:24.852+00:00",[],"Analysis-of-a-new-strain-of-Euphorbia-mosaic-virus-with-distinct-replication-specificity-unveils-a-lineage-of-begomoviruses-with-short-Rep-sequences-in-the-DNA-B-intergenic-region",{"abstract":712,"title":714,"gsPaper":716,"references":717,"doi":719},{"EN":713},"Euphorbia mosaic virus (EuMV) is a member of the SLCV clade, a lineage of New World begomoviruses that display distinctive features in their replication-associated protein (Rep) and virion-strand replication origin. The first entirely characterized EuMV isolate is native from Yucatan Peninsula, Mexico; subsequently, EuMV was detected in weeds and pepper plants from another region of Mexico, and partial DNA-A sequences revealed significant differences in their putative replication specificity determinants with respect to EuMV-YP. This study was aimed to investigate the replication compatibility between two EuMV isolates from the same country. A new isolate of EuMV was obtained from pepper plants collected at Jalisco, Mexico. Full-length clones of both genomic components of EuMV-Jal were biolistically inoculated into plants of three different species, which developed symptoms indistinguishable from those induced by EuMV-YP. Pseudorecombination experiments with EuMV-Jal and EuMV-YP genomic components demonstrated that these viruses do not form infectious reassortants in Nicotiana benthamiana, presumably because of Rep-iteron incompatibility. Sequence analysis of the EuMV-Jal DNA-B intergenic region (IR) led to the unexpected discovery of a 35-nt-long sequence that is identical to a segment of the rep gene in the cognate viral DNA-A. Similar short rep sequences ranging from 35- to 51-nt in length were identified in all EuMV isolates and in three distinct viruses from South America related to EuMV. These short rep sequences in the DNA-B IR are positioned downstream to a ~160-nt non-coding domain highly similar to the CP promoter of begomoviruses belonging to the SLCV clade. EuMV strains are not compatible in replication, indicating that this begomovirus species probably is not a replicating lineage in nature. The genomic analysis of EuMV-Jal led to the discovery of a subgroup of SLCV clade viruses that contain in the non-coding region of their DNA-B component, short rep gene sequences located downstream to a CP-promoter-like domain. This assemblage of DNA-A-related sequences within the DNA-B IR is reminiscent of polyomavirus microRNAs and could be involved in the posttranscriptional regulation of the cognate viral rep gene, an intriguing possibility that should be experimentally explored",{"EN":715},"Analysis of a new strain of Euphorbia mosaic virus with distinct replication specificity unveils a lineage of begomoviruses with short Rep sequences in the DNA-B intergenic region",{"VOID":304},{"VOID":718},"Hanley-Bowdoin L, Settlage SB, Orozco BM, Nagar S, Robertson D: Geminiviruses: models for plant DNA replication, transcription, and cell cycle regulation. Crit Rev Plant Sci 1999, 18: 71-106. 10.1016\u002FS0735-2689(99)00383-4\nZhang W, Olson NH, Baker TS, Faulkner L, Agbandje-McKenna M, Boulton MI, Davies JW, McKenna R: Structure of the Maize streak virus geminate particle. 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Annu Rev Plant Physiol Plant Mol Biol 1998, 49: 525-555. 10.1146\u002Fannurev.arplant.49.1.525\nHernandez-Zepeda C, Brown JK, Moreno-Valenzuela OA, Arguello-Astorga G, Idris AM, Carnevali G, Rivera-Bustamante RF: Characterization of Rhynchosia yellow mosaic Yucatan virus , a new recombinant begomovirus associated with two fabaceous weeds in Yucatan, Mexico. Arch Virol 2010, 155: 1571-1579. 10.1007\u002Fs00705-010-0730-0\nLescot M, Déhais P, Moreau Y, De Moor B, Rouzé P, Rombauts S: PlantCARE: a database of plant cis -acting regulatory elements and a portal to tools for in silico analysis of promoter sequences. Nucleic Acids Res 2002, 30: 325-327. 10.1093\u002Fnar\u002F30.1.325\nHigo K, Ugawa Y, Iwamoto M, Korenaga T: Plant cis -acting regulatory DNA elements (PLACE) database:1999. Nucleic Acids Research 1999, 27: 297-300. 10.1093\u002Fnar\u002F27.1.297\nRuiz-Medrano R, Guevara-Gonzalez RG, Arguello-Astorga GR, Monsalve-Fonnegra Z, Herrera-Estrella LR, Rivera-Bustamante RF: Identification of a sequence element involved in AC2-mediated transactivation of the Pepper huasteco virus coat protein gene. Virology 1999, 253: 162-169. 10.1006\u002Fviro.1998.9484\nItzhaki H, Maxson JM, Woodson WR: An ethylene-responsive enhancer element is involved in the senescence-related expression of the carnation glutathione-S transferase (GST1) gene. Proc Natl Acad Sci USA 1994, 91: 8925-8929. 10.1073\u002Fpnas.91.19.8925\nMontgomery J, Goldman S, Deikman J, Margossian L, Fischer RL: Identification of an ethylene responsive region in the promoter of a fruit ripening gene. Proc Natl Acad Sci USA 1993, 90: 5939-5943. 10.1073\u002Fpnas.90.13.5939\nRawat R, Xu Z-F, Yao K-M, Chye ML: Identification of cis-elements for ethylene and circadian regulation of the Solanum melongena gene encoding cysteine proteinase. Plant Mol Biol 2005, 57: 629-643. 10.1007\u002Fs11103-005-0954-7\nPetty ITD, Coutts RHA, Buck KW: Transcriptional mapping of the coat protein gene of tomato golden mosaic virus. J Gen Virol 1988, 69: 1359-1365. 10.1099\u002F0022-1317-69-6-1359\nPaprotka T, Metzler V, Jeske H: The first DNA 1-like alpha satellites in association with New World begomoviruses in natural infections. Virology 2010, 404: 148-157. 10.1016\u002Fj.virol.2010.05.003\nHanson SF, Hoogstraten RA, Ahlquist P, Gilbertson RL, Russell DR, Maxwell DP: Mutational analysis of a putative NTP-binding domain in the replication-associated protein (AC1) of Bean golden mosaic geminivirus. Virology 1995, 211: 1-9. 10.1006\u002Fviro.1995.1373\nKoonin EugeneV: A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication. Nucleic Acids Res 1993, 21: 2541-2547. 10.1093\u002Fnar\u002F21.11.2541\nCazzonelli CI, Burke J, Velten J: Functional characterization of the geminiviral conserved late element (CLE) in uninfected tobacco. Plant Mol Biol 2005, 58: 465-81. 10.1007\u002Fs11103-005-6589-x\nVelten J, Morey KJ, Cazzonelli CI: Plant viral intergenic DNA sequence repeats with transcription enhancing activity. Virol J 2005, 2: 16-24. 10.1186\u002F1743-422X-2-16\nEagle PA, Hanley-Bowdoin L: Cis elements that contribute to geminivirus transcriptional regulation and the efficiency of DNA replication. J Virol 1997, 71: 6947-6955.\nGibbs AJ, Gibbs MJ: A broader definition of the virus species. Arch Virol 2006, 151: 1419-1422. 10.1007\u002Fs00705-006-0775-2\nVan Regenmortel MH: Applying the species concept to plant viruses. Arch Virol 1989, 104: 1-17. 10.1007\u002FBF01313804\nChatterji A, Padidam M, Beachy RN, Fauquet CM: Identification of replication specificity determinance in tomato leaf curl virus from New Delhi. J Virol 1999, 73: 5481-5489.\nPadidam M, Beachy RN, Fauquet CM: Tomato leaf curl geminivirus from India has a bipartite genome and coat protein is not essential for infectivity. J Gen Virol 1995, 76: 25-35. 10.1099\u002F0022-1317-76-1-25\nLefeuvre P, Lett JM, Varsani A, Martin DP: Widely conserved recombination patterns among single-stranded DNA viruses. J Virol 2009, 83: 2697-707. 10.1128\u002FJVI.02152-08\nLefeuvre P, Lett JM, Reynaud B, Martin DP: Avoidance of protein fold disruption in natural virus recombinants. PLoS Pathog 2007, 3: e181. 10.1371\u002Fjournal.ppat.0030181\nVarsani A, Shepherd DN, Monjane AL, Owor BE, Erdmann JB, Rybicki EP, Peterschmitt M, Briddon RW, Markham PG, Oluwafemi S, Windram OP, Lefeuvre P, Lett JM, Martin DP: Recombination, decreased host specificity and increased mobility may have driven the emergence of maize streak virus as an agricultural pathogen. J Gen Virol 2008, 89: 2063-2074. 10.1099\u002Fvir.0.2008\u002F003590-0\nLondoño A, Riego-Ruiz L, Arguello-Astorga GR: DNA-binding specificity determinants of replication proteins encoded by eukaryotic ssDNA viruses are adjacent to widely separated RCR conserved motifs. Arch Virol 2010, 155: 1033-1046. 10.1007\u002Fs00705-010-0674-4\nBartel DP: MicroRNAs: genomics, biogenesis, mechanism, and function. Cell 2004, 116: 281-297. 10.1016\u002FS0092-8674(04)00045-5\nNair V, Zavolan M: Virus-encoded microRNAs: novel regulators of gene expression. Trends Microbiol 2006, 14: 169-175. 10.1016\u002Fj.tim.2006.02.007\nSkalsky RL, Cullen BR: Viruses, microRNAs, and host interactions. Annu Rev Microbiol 2010, 64: 123-141. 10.1146\u002Fannurev.micro.112408.134243\nSullivan CS, Grundhoff AT, Tevethia S, Pipas JM, Ganem D: SV40-encoded microRNAs regulate viral gene expression and reduce susceptibility to cytotoxic T cells. Nature 2005, 435: 682-686. 10.1038\u002Fnature03576\nCullen BR: Five Questions about Viruses and MicroRNAs. PLoS Pathog 2010, 6: e1000787. 10.1371\u002Fjournal.ppat.1000787\nSeo GJ, Fink LH, O'Hara B, Atwood WJ, Sullivan CS: Evolutionarily conserved function of a viral microRNA. J Virol 2008, 82: 9823-9828. 10.1128\u002FJVI.01144-08\nSullivan CS, Sung CK, Pack CD, Grundhoff A, Lukacher AE: Murine Polyomavirus encodes a microRNA that cleaves early RNA transcripts but is not essential for experimental infection. Virology 2009, 387: 157-167. 10.1016\u002Fj.virol.2009.02.017\nDellaporta SL, Wood J, Hicks JB: A plant DNA minipreparation: version II. Plant Mol Biol Rep 1983, 1: 19-21. 10.1007\u002FBF02712670\nMauricio-Castillo JA, Argüello-Astorga GR, Alpuche-Solís AG, Monreal-Vargas CT, Díaz-Gómez O, de la Torre-Almaraz R: First Report of Tomato severe leaf curl virus in México. Plant Dis 2006, 90: 1116. 10.1094\u002FPD-90-1116A\nCarrillo-Tripp J, Lozoya-Gloria E, Rivera-Bustamante RF: Symptom remission and specific resistance of pepper plants after infection by Pepper golden mosaic virus . Phytopathology 2007, 97: 51-57. 10.1094\u002FPHYTO-97-0051\nAscencio-Ibañez JT, Settlage SB: DNA abrasion onto plants is an effective method for geminivirus infection and virus induced gene silencing. J Virol Met 2007, 142: 198-203. 10.1016\u002Fj.jviromet.2007.01.031\nTamura K, Dudley J, Nei M, Kumar S: MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. 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Virology 2003, 305: 452-462. 10.1006\u002Fviro.2002.1757",{"VOID":720},"10.1186\u002F1743-422X-7-275","2024-09-05T00:27:20.599+00:00","https:\u002F\u002Fvirologyj.biomedcentral.com\u002Farticles\u002F10.1186\u002F1743-422X-7-275",[724,739,754,767,780,795,808,821],{"id":725,"sortIndex":21,"researcher":20,"roles":726,"affiliations":727,"properties":736},"1abaa31c-6a4c-4626-9d37-eab6be685644",[151],[728],{"id":729,"sortIndex":21,"affiliation":730,"properties":20},"93cf7e13-df5a-42ee-b843-03b28435ece0",{"id":729,"createTime":20,"updateTime":20,"relativeEntities":731,"slug":20,"properties":732,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":735,"statistic":20},[],{"title":733},{"VI":734},"Instituto Potosino de Investigación Científica y Tecnológica, A.C.,Camino a la Presa San José,SLP, México",[],{"title":737},{"VI":738},"Josefat 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of full length genomes of herpesviruses as bacterial artificial chromosomes (BAC) has greatly facilitated the manipulation of the genomes of several herpesviruses to identify the pathogenic determinants. We have previously reported the construction of the BAC clone (pRB-1B5) of the highly oncogenic Marek's disease virus (MDV) strain RB-1B, which has proven to be a valuable resource for elucidating several oncogenic determinants. Despite the retention of the BAC replicon within the genome, the reconstituted virus was able to induce tumours in susceptible chickens. Nevertheless, it was unclear whether the presence of the BAC influenced the full oncogenic potential of the reconstituted virus. To maximize the closeness of BAC-derived virus to the parental RB-1B strain, we modified the existing pRB-1B5 clone by restoring the Us2 and by introducing SV40-cre cassette within the lox P sites of the mini-F plasmid, to allow self-excision of the plasmid sequences in chicken cells. The reconstituted virus from the modified clone showed significant improvement in replication in vitro and in vivo. Excision of the BAC sequences also enhanced the pathogenicity to levels similar to that of the parental virus, as the cumulative incidence of Marek's disease in groups infected with the recombinant and the parental viruses showed no significant differences. Thus, we have been able to make significant improvements to the existing BAC clone of this highly oncogenic virus which would certainly increase its usefulness as a valuable tool for studies on identifying the oncogenic determinants of this major avian pathogen.",{"EN":899},"Self-excision of the BAC sequences from the recombinant Marek's disease virus genome increases replication and pathogenicity",{"VOID":901},"[\"11119669118418749444\"]",{"VOID":903},"Calnek BW: Pathogenesis of Marek's disease virus infection. Curr Top Microbiol Immunol 2001, 255: 25-55.\nDavison F, Nair V: Marek's disease: An Evolving Problem. London: Elsevier Academic Press; 2004.\nMorrow C, Fehler F: Marek's disease: a worldwide problem. In Marek's disease, An Evolving Problem. Edited by: Davison F, Nair V. Oxford: Elsevier Academic Press; 2004:49-61. [Pastoret P-P (Series Editor): Biology of animal infections].\nCalnek BW: Marek's disease: a model for herpesvirus oncology. CRC Crit Rev Microbiol 1986, 12: 293-320.\nOsterrieder N, Kamil JP, Schumacher D, Tischer BK, Trapp S: Marek's disease virus: from miasma to model. Nat Rev Micro 2006, 4: 283-294. 10.1038\u002Fnrmicro1382\nOsterrieder K, Vautherot JF: The genome content of Marek's disease-like viruses. In Marek's disease, An Evolving Problem. Edited by: Davison F, Nair V. Oxford: Elsevier Academic Press; 2004:17-31. [Pastoret P-P (Series Editor): Biology of animal infections].\nZelnik V: Marek's disease virus research in the post-sequencing era: new tools for the study of gene functions and virus-host interactions. Avian Pathol 2003, 32: 323-334. 10.1080\u002F0307945031000121068\nSchumacher D, Tischer BK, Fuchs W, Osterrieder N: Reconstitution of Marek's disease virus serotype 1 (MDV-1) from DNA cloned as a bacterial artificial chromosome and characterization of a glycoprotein B-negative MDV-1 mutant. J Virol 2000, 74: 11088-11098. 10.1128\u002FJVI.74.23.11088-11098.2000\nTischer BK, von Einem J, Kaufer B, Osterrieder N: Two-step Red-mediated recombination for versatile, high-efficiency markerless DNA manipulation in Escherichia coli. BioTechniques 2006, 40: 1-6.\nSchat KA, Calnek BW, Fabricant J: Characterisation of two highly oncogenic strains of Marek's disease virus. Avian Pathol 1982, 11: 593-605. 10.1080\u002F03079458208436134\nPetherbridge L, Brown AC, Baigent SJ, Howes K, Sacco MA, Osterrieder N, Nair VK: Oncogenicity of virulent Marek's disease virus cloned as bacterial artificial chromosomes. J Virol 2004, 78: 13376-13380. 10.1128\u002FJVI.78.23.13376-13380.2004\nBrown AC, Baigent SJ, Smith LP, Chattoo JP, Petherbridge LJ, Hawes P, Allday MJ, Nair V: Interaction of MEQ protein and C-terminal-binding protein is critical for induction of lymphomas by Marek's disease virus. PNAS 2006, 103: 1687-1692. 10.1073\u002Fpnas.0507595103\nJarosinski KW, Osterrieder N, Nair VK, Schat KA: Attenuation of Marek's Disease Virus by Deletion of Open Reading Frame RLORF4 but Not RLORF5a. J Virol 2005, 79: 11647-11659. 10.1128\u002FJVI.79.18.11647-11659.2005\nKamil JP, Tischer BK, Trapp S, Nair VK, Osterrieder N, Kung HJ: vLIP, a viral lipase homologue, is a virulence factor of Marek's disease virus. J Virol 2005, 79: 6984-6996. 10.1128\u002FJVI.79.11.6984-6996.2005\nTrapp S, Parcells MS, Kamil JP, Schumacher D, Tischer BK, Kumar PM, Nair VK, Osterrieder N: A virus-encoded telomerase RNA promotes malignant T cell lymphomagenesis. J Exp Med 2006, 203: 1307-1317. 10.1084\u002Fjem.20052240\nSmith GA, Enquist LW: A self-recombining bacterial artificial chromosome and its application for analysis of herpesvirus pathogenesis. Proc Natl Acad Sci USA 2000, 97: 4873-4878. 10.1073\u002Fpnas.080502497\nYu D, Smith GA, Enquist LW, Shenk T: Construction of a self-excisable bacterial artificial chromosome containing the human cytomegalovirus genome and mutagenesis of the diploid TRL\u002FIRL13 gene. J Virol 2002, 76: 2316-2328. 10.1128\u002Fjvi.76.5.2316-2328.2002\nChang WL, Barry PA: Cloning of the full-length rhesus cytomegalovirus genome as an infectious and self-excisable bacterial artificial chromosome for analysis of viral pathogenesis. J Virol 2003, 77: 5073-5083. 10.1128\u002FJVI.77.9.5073-5083.2003\nLee EC, Yu D, Martinez de Velasco J, Tessarollo L, Swing DA, Court DL, Jenkins NA, Copeland NG: A highly efficient Escherichia coli-based chromosome engineering system adapted for recombinogenic targeting and subcloning of BAC DNA. Genomics 2001, 73: 56-65. 10.1006\u002Fgeno.2000.6451\nBaigent SJ, Petherbridge LJ, Howes K, Smith LP, Currie RJ, Nair VK: Absolute quantitation of Marek's disease virus genome copy number in chicken feather and lymphocyte samples using real-time PCR. J Virol Methods 2005, 123: 53-64. 10.1016\u002Fj.jviromet.2004.08.019\nAltman DG: Practical Statistics for Medical Research. London: Chapman and Hall; 1991.\nJarosinski KW, Margulis NG, Kamil JP, Spatz SJ, Nair VK, Osterrieder N: Horizontal transmission of Marek's disease virus requires US2, the UL13 protein kinase, and gC. 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Src family tyrosine kinases (SFK) are cellular regulatory proteins that influence cell adhesion, proliferation, invasion and survival during tumor development. Elevated activity of Src was associated with increased cell proliferation and invasivity in human papillomavirus (HPV)-associated malignancies; therefore, transduced human foreskin keratinocytes (HFK) were used to investigate whether SFK activation is a downstream effect of papillomaviral oncoproteins. Activation of ubiquitously expressed SFKs, namely Src, Yes and Fyn, was investigated in both proliferating and differentiating keratinocytes. In proliferating keratinocytes, Src, Yes and Fyn mRNA levels were not affected by HPV 16 E6 or E7 oncoproteins, while at the protein level as detected by western blot, the presence of both E6 and E7 resulted in substantial increase in Src and Yes expression, but did not alter the high constitutive level of Fyn. Phospo-kinase array revealed that all ubiquitously expressed SFKs are activated by phosphorylation in the presence of HPV 16 E7 oncoprotein. Keratinocyte differentiation led to increased Yes mRNA and protein levels in all transduced cell lines, while it did not influence the Src transcription but resulted in elevated Src protein level in HPV16 E7 expressing lines. This study revealed that HPV 16 oncoproteins upregulate Src family kinases Src and Yes via posttranscriptional mechanisms. A further effect of HPV 16 E7 oncoprotein is to enhance the activating phosphorylation of SFKs expressed in keratinocytes.",{"EN":1048},"Activation of Src, Fyn and Yes non-receptor tyrosine kinases in keratinocytes expressing human papillomavirus (HPV) type 16 E7 oncoprotein",{"VOID":1050},"[\"10085619131216004075\"]",{"EN":1052},"",{"VOID":1054},"Bradshaw JM: The Src, Syk, and Tec family kinases: Distinct types of molecular switches. Cell Signal 2010, 22: 1175-1184. 10.1016\u002Fj.cellsig.2010.03.001\nCabodi S, Di Stefano P, Leal MDC, Tinnirello A, Bisaro B, Morello V: Integrins and signal transduction. Integrins and Ion Channels: Molecular Complexes and Signaling 2010, 674: 43-54. 10.1007\u002F978-1-4419-6066-5_5\nKim LC, Song LX, Haura EB: Src kinases as therapeutic targets for cancer. Nat Rev Clin Oncol 2009, 6: 587-595. 10.1038\u002Fnrclinonc.2009.129\nRoskoski R: Src protein-tyrosine kinase structure and regulation. Biochem Biophys Res Commun 2004, 324: 1155-1164. 10.1016\u002Fj.bbrc.2004.09.171\nRoskoski R: Src kinase regulation by phosphorylation and dephosphorylation. Biochem Biophys Res Commun 2005, 331: 1-14. 10.1016\u002Fj.bbrc.2005.03.012\nGuarino M: Src signaling in cancer invasion. J Cell Physiol 2010, 223: 14-26.\nSen B, Johnson FM: Regulation of SRC family kinases in human cancers. J Signal Transduct 2011,201(1):865819.\nSummy JM, Gallick GE: Src family kinases in tumor progression and metastasis. Cancer Metastasis Rev 2003, 22: 337-358. 10.1023\u002FA:1023772912750\nHamamura K, Tsuji M, Hotta H, Ohkawa Y, Takahashi M, Shibuya H: Functional activation of Src family kinase Yes protein is essential for the enhanced malignant properties of human melanoma cells expressing ganglioside GD3. J Biol Chem 2011, 286: 18526-18537. 10.1074\u002Fjbc.M110.164798\nKluger HM, Dudek AZ, McCann C, Ritacco J, Southard N, Jilaveanu LB: A phase 2 trial of dasatinib in advanced melanoma. Cancer 2011, 117: 2202-2208. 10.1002\u002Fcncr.25766\nKonecny GE, Glas R, Dering J, Manivong K, Qi J, Finn RS: Activity of the multikinase inhibitor dasatinib against ovarian cancer cells. Br J Cancer 2009, 101: 1699-1708. 10.1038\u002Fsj.bjc.6605381\nLee JH, Pyon JK, Kim DW, Lee SH, Nam HS, Kim CH: Elevated c-Src and c-Yes expression in malignant skin cancers. J Exp Clin Cancer Res 2010, 29: 116. 10.1186\u002F1756-9966-29-116\nMontero JC, Seoane S, Ocana A, Pandiella A: Inhibition of Src family kinases and receptor tyrosine kinases by dasatinib: possible combinations in solid tumors. Clin Cancer Res 2011, 17: 5546-5552. 10.1158\u002F1078-0432.CCR-10-2616\nSaito YD, Jensen AR, Salgia R, Posadas EM: Fyn a novel molecular target in cancer. Cancer 2010, 116: 1629-1637. 10.1002\u002Fcncr.24879\nTamm C, Galito SP, Anneren C: Differential effects on cell motility, embryonic stem cell self-renewal and senescence by diverse Src kinase family inhibitors. Exp Cell Res 2012, 318: 336-349. 10.1016\u002Fj.yexcr.2011.12.008\nKong L, Deng ZH, Zhao YZ, Wang YM, Sarkar FH, Zhang YX: Down-regulation of phospho-non-receptor Src tyrosine kinases contributes to growth inhibition of cervical cancer cells. Med Oncol 2011, 28: 1495-1506. 10.1007\u002Fs12032-010-9583-3\nKong L, Deng ZH, Shen HY, Zhang YX: Src family kinase inhibitor PP2 efficiently inhibits cervical cancer cell proliferation through down-regulating phospho-Src-Y416 and phospho-EGFR-Y1173. Mol Cell Biochem 2011, 348: 11-19. 10.1007\u002Fs11010-010-0632-1\nYasmeen A, Alachkar A, Dekhil H, Gambacorti-Passerini C, Al Moustafa AE: Locking Src\u002FAbl Tyrosine Kinase Activities Regulate Cell Differentiation and Invasion of Human Cervical Cancer Cells Expressing E6\u002FE7 Oncoproteins of High-Risk HPV. J Oncol 2010,2010(530130):10.\nAl Moustafa AE, Yasmeen A, Achkhar A: Src inhibitors are promising therapy molecules for human cervical carcinomas. Med Hypotheses 2011, 77: 812-814. 10.1016\u002Fj.mehy.2011.07.043\nFaridi R, Zahra A, Khan K, Idrees M: Oncogenic potential of human papillomavirus (HPV) and its relation with cervical cancer. Virol J 2011, 8: 269. 10.1186\u002F1743-422X-8-269\nMunger K, Howley PM: Human papillomavirus immortalization and transformation functions. Virus Res 2002, 89: 213-228. 10.1016\u002FS0168-1702(02)00190-9\nKajitani N, Satsuka A, Kawate A, Sakai H: Productive lifecycle of human papillomaviruses that depends upon squamous epithelial differentiation. Front Microbiol 2012, 3: 152.\nKorzeniewski N, Spardy N, Duensing A, Duensing S: Genomic instability and cancer: lessons learned from human papillomaviruses. Cancer Lett 2011, 305: 113-122. 10.1016\u002Fj.canlet.2010.10.013\nCardeal LBD, Boccardo E, Termini L, Rabachini T, Andreoli MA, di Loreto C: HPV16 Oncoproteins Induce MMPs\u002FRECK-TIMP-2 Imbalance in Primary Keratinocytes: Possible Implications in Cervical Carcinogenesis. PLoS One 2012, 7: e33585. 10.1371\u002Fjournal.pone.0033585\nMoody CA, Laimins LA: Human papillomavirus oncoproteins: pathways to transformation. Nat Rev Cancer 2010, 10: 550-560. 10.1038\u002Fnrc2886\nGyongyosi E, Szalmas A, Ferenczi A, Konya J, Gergely L, Veress G: Effects of human papillomavirus (HPV) type 16 oncoproteins on the expression of involucrin in human keratinocytes. Virol J 2012, 9: 36. 10.1186\u002F1743-422X-9-36\nSancier F, Dumont A, Sirvent A, de Plater LP, Edmonds T, David G: Specific oncogenic activity of the Src-family tyrosine kinase c-Yes in colon carcinoma cells. PLoS One 2011, 6: e17237. 10.1371\u002Fjournal.pone.0017237\nCheng S, Schmidtgrimminger DC, Murant T, Broker TR, Chow LT: Differentiation-dependent Up-regulation of the human papillomavirus E7 gene reactivates cellular Dna-replication in suprabasal differentiated keratinocytes. Genes Dev 1995, 9: 2335-2349. 10.1101\u002Fgad.9.19.2335\nPyeon D, Pearce SM, Lank SM, Ahlquist P, Lambert PF: Establishment of human papillomavirus infection requires cell cycle progression. PLoS Pathog 2009, 5: e1000318. 10.1371\u002Fjournal.ppat.1000318\nContreras-Paredes A, Cruz-Hernandez E, Martinez-Ramirez I, Duenas-Gonzalez A, Lizano M: E6 variants of human papillomavirus 18 differentially modulate the protein kinase B\u002Fphosphatidylinositol 3-kinase (akt\u002FPI3K) signaling pathway. Virology 2009, 383: 78-85. 10.1016\u002Fj.virol.2008.09.040\nMantovani F, Banks L: The human papillomavirus E6 protein and its contribution to malignant progression. Oncogene 2001, 20: 7874-7887. 10.1038\u002Fsj.onc.1204869\nMunger K, Basile JR, Duensing S, Eichten A, Gonzalez SL, Grace M: Biological activities and molecular targets of the human papillomavirus E7 oncoprotein. Oncogene 2001, 20: 7888-7898. 10.1038\u002Fsj.onc.1204860\nBaldwin A, Li WL, Grace M, Pearlberg J, Harlow E, Munger K: Kinase requirements in human cells: II. Genetic interaction screens identify kinase requirements following HPV16 E7 expression in cancer cells. Proc Natl Acad Sci USA 2008, 105: 16478-16483. 10.1073\u002Fpnas.0806195105\nArulanandam R, Geletu M, Raptis L: The simian virus 40 large tumor antigen activates cSrc and requires cSrc for full neoplastic transformation. Anticancer Res 2010, 30: 47-53.\nDellas A, Schultheiss E, Almendral AC, Torhorst J, Gudat F: Assessment of EGFR and TGF-alpha expression in relationship to HPV status and KI-67 distribution in cervical intraepithelial neoplasms. Int J Cancer 1996, 69: 165-169. 10.1002\u002F(SICI)1097-0215(19960621)69:3\u003C165::AID-IJC2>3.0.CO;2-Y\nMcCormack SJ, Brazinski SE, Moore JL, Werness BA, Goldstein DJ: Activation of the focal adhesion kinase signal transduction pathway in cervical carcinoma cell lines and human genital epithelial cells immortalized with human papillomavirus type 18. Oncogene 1997, 15: 265-274. 10.1038\u002Fsj.onc.1201186\nKasai A, Shima T, Okada M: Role of Src family tyrosine kinases in the down-regulation of epidermal growth factor signaling in PC12 cells. Genes Cells 2005, 10: 1175-1187. 10.1111\u002Fj.1365-2443.2005.00909.x\nThelemann A, Petti F, Griffin G, Iwata K, Hunt T, Settinari T: Phosphotyrosine signaling networks in epidermal growth factor receptor overexpressing squamous carcinoma cells. Mol Cell Proteomics 2005, 4: 356-376. 10.1074\u002Fmcp.M400118-MCP200\nWeis S, Cui JH, Cheresh D: Unexpected role for VEGF-mediated vascular permeability in tumor cell extravasation and metastasis. J Histochem Cytochem 2004, 52: S12.\nZhao J, Guan JL: Signal transduction by focal adhesion kinase in cancer. 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Binding properties, cell delivery, and gene transfer of adenoviral penton base displaying bacteriophage. Virology. 2001;282:102–12.",{"doi":1999},"10.1006\u002Fviro.2000.0809",{"id":20,"text":2001,"url":20,"identifiers":2002},"Li Z, Zhang J, Zhao R, Xu Y, Gu J. Preparation of peptide-targeted phagemid particles using a protein III-modified helper phage. BioTechniques. 2005;39:493–7.",{"doi":2003},"10.2144\u002F000112007",{"id":20,"text":2005,"url":20,"identifiers":2006},"Banerjee D, Liu AP, Voss NR, Schmid SL, Finn MG. Multivalent display and receptor-mediated endocytosis of transferrin on virus-like particles. Chembiochem. 2010;11:1273–9.",{"doi":2007},"10.1002\u002Fcbic.201000125",{"id":20,"text":2009,"url":20,"identifiers":2010},"Studier FW, Moffatt BA. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol. 1986;189:113–30.",{"doi":2011},"10.1016\u002F0022-2836(86)90385-2",{"id":20,"text":2013,"url":20,"identifiers":2014},"Xu H, Bao X, Lu Y, Liu Y, Deng B, Wang Y, Xu Y, Hou J. Immunogenicity of T7 bacteriophage nanoparticles displaying G-H loop of foot-and-mouth disease virus (FMDV). Vet Microbiol. 2017;205:46–52.",{"doi":2015},"10.1016\u002Fj.vetmic.2017.04.023",{"id":20,"text":2017,"url":20,"identifiers":2018},"Liu SG, Tobias R, McClure S, Styba G, Shi QW, Jackowski E. Removal of endotoxin from recombinant protein preparations. Clin Biochem. 1997;30:455–63.",{"doi":2019},"10.1016\u002FS0009-9120(97)00049-0",{"id":20,"text":2021,"url":20,"identifiers":2022},"Hashemi H, Pouyanfard S, Bandehpour M, Mahmoudi M, Bernasconi M, Kazemi B, Mokhtari-Azad T. Efficient endotoxin removal from T7 phage preparations by a mild detergent treatment followed by ultrafiltration. Acta Virol. 2013;57:373–4.",{},{"id":20,"text":2024,"url":20,"identifiers":2025},"Frampton RA, Acedo EL, Young VL, Chen D, Tong B, Taylor C, Easingwood RA, Pitman AR, Kleffmann T, Bostina M, Fineran PC. Genome, proteome and structure of a T7-like bacteriophage of the kiwifruit canker Phytopathogen pseudomonas syringae pv. Actinidiae. Viruses. 2015;7:3361–79.",{"doi":2026},"10.3390\u002Fv7072776",{"id":20,"text":2028,"url":20,"identifiers":2029},"Fagbohun OA, Bedi D, Grabchenko NI, Deinnocentes PA, Bird RC, Petrenko VA. Landscape phages and their fusion proteins targeted to breast cancer cells. Protein Eng Des Sel. 2012;25:271–83.",{"doi":2030},"10.1093\u002Fprotein\u002Fgzs013",{"id":20,"text":2032,"url":20,"identifiers":2033},"Gillespie JW, Wei L, Petrenko VA. Selection of lung cancer-specific landscape phage for targeted drug delivery. Comb Chem High Throughput Screen. 2016;19:412–22.",{"doi":2034},"10.2174\u002F1386207319666160420141024",{"id":20,"text":2036,"url":20,"identifiers":2037},"Wadia J, Eguchi A, Dowdy SF. DNA delivery into mammalian cells using bacteriophage lambda displaying the TAT transduction domain. Cold Spring Harb Protoc. 2013;2013:59–65.",{"doi":2038},"10.1101\u002Fpdb.prot072660",{"id":20,"text":2040,"url":20,"identifiers":2041},"Eguchi A, Akuta T, Okuyama H, Senda T, Yokoi H, Inokuchi H, Fujita S, Hayakawa T, Takeda K, Hasegawa M, Nakanishi M. Protein transduction domain of HIV-1 tat protein promotes efficient delivery of DNA into mammalian cells. J Biol Chem. 2001;276:26204–10.",{"doi":2042},"10.1074\u002Fjbc.M010625200",{"id":20,"text":2044,"url":20,"identifiers":2045},"Kim A, Shin TH, Shin SM, Pham CD, Choi DK, Kwon MH, Kim YS. Cellular internalization mechanism and intracellular trafficking of filamentous M13 phages displaying a cell-penetrating transbody and TAT peptide. PLoS One. 2012;7:e51813.",{"doi":2046},"10.1371\u002Fjournal.pone.0051813",{"id":20,"text":2048,"url":20,"identifiers":2049},"Liu Y, Jones M, Hingtgen CM, Bu G, Laribee N, Tanzi RE, Moir RD, Nath A, He JJ. Uptake of HIV-1 tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands. Nat Med. 2000;6:1380–7.",{"doi":2050},"10.1038\u002F82199",{"id":20,"text":2052,"url":20,"identifiers":2053},"Vives E, Brodin P, Lebleu B. A truncated HIV-1 tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J Biol Chem. 1997;272:16010–7.",{"doi":2054},"10.1074\u002Fjbc.272.25.16010",{"id":2056,"createTime":2057,"updateTime":2058,"relativeEntities":2059,"slug":2060,"properties":2061,"entityType":142,"verifyStatus":143,"verifyTime":2071,"verifyNote":145,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":2072,"fullTextUrl":20,"authors":2073,"publicationType":233,"publisherRelationship":2141,"citationCount":20,"citationInfo":20,"publishDate":2192,"publishYear":1234,"citationAnalyzeStatus":533,"lastCitationAnalyze":2193,"indexDatabases":2194,"openAccess":20,"references":20,"isForceReanalyzing":289},"e141be56-3eb0-4a64-8157-26eb8da60fb4","2024-01-15T04:11:24.518+00:00","2026-07-27T10:43:19.962+00:00",[],"Simultaneous-detection-and-differentiation-of-Rice-black-streaked-dwarf-virus-RBSDV-and-Southern-rice-black-streaked-dwarf-virus-SRBSDV-by-duplex-real-time-RT-PCR",{"abstract":2062,"title":2064,"gsPaper":2066,"references":2067,"doi":2069},{"EN":2063},"The diseases caused by Rice black streaked dwarf virus (RBSDV) and Southern rice black streaked dwarf virus (SRBSDV) have been occurring epidemically in China and southeastern Asia in recent years. A sensitive, reliable and quantitative method is required to detect and distinguish for RBSDV and SRBSDV in rice and vector insects. We developed a sensitive and lineage-specific duplex real time RT-qPCR for detection of RBSDV and SRBSDV in a single or\u002Fand double infection in rice samples. The duplex RT-qPCR was optimized using standard samples transcribed by T7 Large Scale RNA Production System in vitro. We developed a reliable system for duplex RT-qPCR, in which its co-efficiency of RBSDV and SRBSDV, were 91.6% and 90.7%, respectively. The coefficient of determination was more than 0.990; the slope of linear equation was −3.542, and −3.567, respectively. Out of 30 samples collected in North and Central China, which were suspected to be infected with these two viruses, 10 samples were detected RBSDV positive by RT-PCR and 12 samples by RT-qPCR. No mixed infections were found. Simultaneously, out of total 60 samples collected from Southern China, which were also suspected to be infected with these two viruses, 41 samples were determined SRBSDV positive by RT-PCR and 47 samples by RT-qPCR. Also in this case no mixed infections were found. The rice genes eEF-1a and UBQ5 were selected as internal controls for quantification assay also performed as good expression stability. The duplex RT-qPCR assay provided as a sufficiently sensitive, specific, accurate, reproducible and rapid tool for the detection and differentiation of RBSDV and SRBSDV. The RT-qPCR assay can be used in routine diagnostic of these two viruses in order to study the disease epidemiology in rice crops.",{"EN":2065},"Simultaneous detection and differentiation of Rice black streaked dwarf virus (RBSDV) and Southern rice black streaked dwarf virus (SRBSDV) by duplex real time RT-PCR",{"VOID":304},{"VOID":2068},"Hibino H: Biology and epidemiology of rice viruses. 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J Virol 2012, 86: 5800-5807. 10.1128\u002FJVI.07121-11\nLi L, Li H, Dong H, Wang X, Zhou G: Transmission by Laodelphax striatellus Fallen of Rice black-streaked dwarf virus from frozen infected rice leaves to healthy plants of rice and maize. J Phytopathol 2011, 159: 165. 10.1111\u002Fj.1439-0434.2010.01742.x\nWang Q, Zhou GH, Zhang SG: Detection of Southern rice black-streaked dwarf virus using one-step dual RT-PCR. Acta Phytopathol Sin 2012, 42: 84-87. in Chinese\nZhou T, Du L, Fan Y, Zhou Y: Reverse transcription loop mediated isothermal amplification of RNA for sensitive and rapid detection of southern rice black-streaked dwarf virus. J Virol Methods 2012, 180: 91-95. 10.1016\u002Fj.jviromet.2011.12.014\nChen Z, Yin C, Liu J, Zeng M, Wang Z, Yu D, Bi L, Jin L, Yang S, Song B: Methodology for antibody preparation and detection of southern rice black-streaked dwarf virus. 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J Virol Methods 2000, 88: 1-8. 10.1016\u002FS0166-0934(00)00156-7\nZhang X, Wang X, Zhou G: A one-step real time RT-PCR assay for quantifying rice stripe virus (RSV) in rice and in the small brown planthopper ( Laodelphax striatellus Fallen). J Virol Methods 2008, 151: 181-187. 10.1016\u002Fj.jviromet.2008.05.024\nZhang X, Zhou G, Wang X: Detection of Wheat dwarf virus (WDV) in wheat and vector leafhopper (Psammotetix striatus L.) by real-time PCR. J Virol Methods 2010, 169: 416-419. 10.1016\u002Fj.jviromet.2010.07.029\nSchmittgen TD, Livak KJ: Analyzing real-time PCR data by the comparative CT method. Nat Protoc 2008, 3: 1101-1108. 10.1038\u002Fnprot.2008.73\nLee C, Kim J, Shin SG, Hwang S: Absolute and relative QPCR quantification of plasmid copy number in Escherichia coli . J Biotechnol 2006, 123: 273-280. 10.1016\u002Fj.jbiotec.2005.11.014\nJain M, Nijhawan A, Tyagi AK, Khurana JP: Validation of housekeeping genes as internal control for studying gene expression in rice by quantitative real-time PCR. Biochem Bioph Res Co 2006, 345: 646-651. 10.1016\u002Fj.bbrc.2006.04.140\nGadiou S, Ripl J, Jaňourová B, Jarošová J, Kundu JK: Real-time PCR assay for the discrimination and quantification of wheat and barley strains of Wheat dwarf virus . Virus Genes 2012, 44: 349-355. 10.1007\u002Fs11262-011-0699-0\nRuiz–Ruiz S, Ambrós S, Vives MC, Navarro L, Moreno P, Guerri J: Detection and quantitation of Citrus leaf blotch virus by TaqMan real-time RT-PCR. J Virol Methods 2009, 160: 57-62. 10.1016\u002Fj.jviromet.2009.04.012\nDenno RF, Roderick GK: Population biology of planthoppers. Annu Rev Entomol 1990, 35: 489-520. 10.1146\u002Fannurev.en.35.010190.002421\nZhang SX, Li L, Wang XF, Zhou GH: Transmission of Rice stripe virus acquired from frozen infected leaves by the small brown planthopper ( Laodelphax striatellus Fallen). J Virol Methods 2007, 146: 359-362. 10.1016\u002Fj.jviromet.2007.05.028\nShen JH, Shang JM, Liu GJ: Management of the white-backed planthopper, Sogatella furcifera in China: a mini-review. Chin J Rice Sci 2003,17(S):7-22. in Chinese\nBao YX, Xu XY, Wang JQ, Wang C, Miu Q, Zhai B: Analysis of the atmospheric dynamical backgrounds for the great immigration events of white backed planthopper ( Sogatella furcifera ). Acta Ecol Sin 2007, 27: 4527-4535. in Chinese\nWang YK, Zhai BP: Re-migration capacity of the white-backed planthopper, Sogatella furcifera . Acta Entomol Sin 2004, 47: 467-473. 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motility refers to the peristalsis and contractility of gastrointestinal muscles, including the force and frequency of gastrointestinal muscle contraction. Gastrointestinal motility maintains the normal digestive function of the human body and is a critical component of the physiological function of the digestive tract. At present, gastrointestinal motility disorder-related diseases are gradually affecting human production and life. In recent years, it has been consistently reported that the enteric nervous system has a coordinating and controlling role in gastrointestinal motility. Motility disorders are closely related to functional or anatomical changes in the gastrointestinal nervous system. At the same time, some viral infections, such as herpes simplex virus and varicella-zoster virus infections, can cause damage to the gastrointestinal nervous system. Therefore, this paper describes the mechanisms of viral infection in the gastrointestinal nervous system and the associated clinical manifestations. Studies have indicated that the means by which viruses can cause the infection of the enteric nervous system are various, including retrograde transport, hematogenous transmission and centrifugal transmission from the central nervous system. When viruses infect the enteric nervous system, they can cause clinical symptoms, such as abdominal pain, abdominal distension, early satiation, belching, diarrhea, and constipation, by recruiting macrophages, lymphocytes and neutrophils and regulating intestinal microbes. The findings of several case‒control studies suggest that viruses are the cause of some gastrointestinal motility disorders. It is concluded that one of the causes of gastrointestinal motility disorders is viral infection of the enteric nervous system. In such disorders, the relationships between viruses and nerves remain to be studied more deeply. Further studies are necessary to evaluate whether prophylactic antiviral therapy is feasible in gastrointestinal motility disorders.\u003C\u002Fjats:p>",{"EN":2207},"The mechanisms of nerve injury caused by viral infection in the occurrence of gastrointestinal motility disorder-related 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