{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T18:18:50Z","timestamp":1791397130629,"version":"4.3.3"},"reference-count":77,"publisher":"Japanese Society of Veterinary Science","issue":"7","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Journal of Veterinary Medical Science","J. Vet. Med. Sci."],"published-print":{"date-parts":[[2016]]},"DOI":"10.1292\/jvms.16-0092","type":"journal-article","created":{"date-parts":[[2016,4,1]],"date-time":"2016-04-01T22:05:24Z","timestamp":1459548324000},"page":"1089-1098","source":"Crossref","is-referenced-by-count":53,"title":["The importance of immune evasion in the pathogenesis of rabies virus"],"prefix":"10.1292","volume":"78","author":[{"given":"Naoto","family":"ITO","sequence":"first","affiliation":[{"name":"Laboratory of Zoonotic Diseases, Faculty of Applied Biological Sciences, Gifu University, 1\u20131 Yanagido, Gifu, Gifu 501\u20131193, Japan"},{"name":"The United Graduate School of Veterinary Sciences, Gifu University, 1\u20131 Yanagido, Gifu, Gifu 501\u20131193, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregory W.","family":"MOSELEY","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, 30 Flemington Rd., The University of Melbourne, Victoria 3010, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Makoto","family":"SUGIYAMA","sequence":"additional","affiliation":[{"name":"Laboratory of Zoonotic Diseases, Faculty of Applied Biological Sciences, Gifu University, 1\u20131 Yanagido, Gifu, Gifu 501\u20131193, Japan"},{"name":"The United Graduate School of Veterinary Sciences, Gifu University, 1\u20131 Yanagido, Gifu, Gifu 501\u20131193, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"122","reference":[{"key":"1","doi-asserted-by":"crossref","unstructured":"1. Audsley, M. D. and Moseley, G. W. 2013. Paramyxovirus evasion of innate immunity: Diverse strategies for common targets. <i>World J. Virol.<\/i> 2: 57\u201370.","DOI":"10.5501\/wjv.v2.i2.57"},{"key":"2","doi-asserted-by":"crossref","unstructured":"2. Baloul, L. and Lafon, M. 2003. Apoptosis and rabies virus neuroinvasion. <i>Biochimie<\/i> 85: 777\u2013788.","DOI":"10.1016\/S0300-9084(03)00137-8"},{"key":"3","doi-asserted-by":"crossref","unstructured":"3. Baloul, L., Camelo, S. and Lafon, M. 2004. Up-regulation of Fas ligand (FasL) in the central nervous system: a mechanism of immune evasion by rabies virus. <i>J. Neurovirol.<\/i> 10: 372\u2013382.","DOI":"10.1080\/13550280490521122"},{"key":"4","doi-asserted-by":"crossref","unstructured":"4. Blondel, D., Kheddache, S., Lahaye, X., Dianoux, L. and Chelbi-Alix, M. K. 2010. Resistance to rabies virus infection conferred by the PMLIV isoform. <i>J. Virol.<\/i> 84: 10719\u201310726.","DOI":"10.1128\/JVI.01286-10"},{"key":"5","doi-asserted-by":"crossref","unstructured":"5. Blondel, D., Regad, T., Poisson, N., Pavie, B., Harper, F., Pandolfi, P. P., De Th\u00e9, H. and Chelbi-Alix, M. K. 2002. Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies. <i>Oncogene<\/i> 21: 7957\u20137970.","DOI":"10.1038\/sj.onc.1205931"},{"key":"6","doi-asserted-by":"crossref","unstructured":"6. Bowie, A. G. and Unterholzner, L. 2008. Viral evasion and subversion of pattern-recognition receptor signalling. <i>Nat. Rev. Immunol.<\/i> 8: 911\u2013922.","DOI":"10.1038\/nri2436"},{"key":"7","doi-asserted-by":"crossref","unstructured":"7. Brice, A. and Moseley, G. W. 2013. Viral interactions with microtubules: orchestrators of host cell biology? <i>Future Virol.<\/i> 8: 229\u2013243.","DOI":"10.2217\/fvl.12.137"},{"key":"8","doi-asserted-by":"crossref","unstructured":"8. Brz\u00f3zka, K., Finke, S. and Conzelmann, K. K. 2005. Identification of the rabies virus alpha\/beta interferon antagonist: phosphoprotein P interferes with phosphorylation of interferon regulatory factor 3. <i>J. Virol.<\/i> 79: 7673\u20137681.","DOI":"10.1128\/JVI.79.12.7673-7681.2005"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9. Brz\u00f3zka, K., Finke, S. and Conzelmann, K. K. 2006. Inhibition of interferon signaling by rabies virus phosphoprotein P: activation-dependent binding of STAT1 and STAT2. <i>J. Virol.<\/i> 80: 2675\u20132683.","DOI":"10.1128\/JVI.80.6.2675-2683.2006"},{"key":"10","doi-asserted-by":"crossref","unstructured":"10. Chai, Q., She, R., Huang, Y. and Fu, Z. F. 2015. Expression of neuronal CXCL10 induced by rabies virus infection initiates infiltration of inflammatory cells, production of chemokines and cytokines, and enhancement of blood-brain barrier permeability. <i>J. Virol.<\/i> 89: 870\u2013876.","DOI":"10.1128\/JVI.02154-14"},{"key":"11","doi-asserted-by":"crossref","unstructured":"11. Chelbi-Alix, M. K., Vidy, A., El Bougrini, J. and Blondel, D. 2006. Rabies viral mechanisms to escape the IFN system: the viral protein P interferes with IRF-3, Stat1, and PML nuclear bodies. <i>J. Interferon Cytokine Res.<\/i> 26: 271\u2013280.","DOI":"10.1089\/jir.2006.26.271"},{"key":"12","doi-asserted-by":"crossref","unstructured":"12. Chenik, M., Chebli, K. and Blondel, D. 1995. Translation initiation at alternate in-frame AUG codons in the rabies virus phosphoprotein mRNA is mediated by a ribosomal leaky scanning mechanism. <i>J. Virol.<\/i> 69: 707\u2013712.","DOI":"10.1128\/JVI.69.2.707-712.1995"},{"key":"13","doi-asserted-by":"crossref","unstructured":"13. Chopy, D., Detje, C. N., Lafage, M., Kalinke, U. and Lafon, M. 2011. The type I interferon response bridles rabies virus infection and reduces pathogenicity. <i>J. Neurovirol.<\/i> 17: 353\u2013367.","DOI":"10.1007\/s13365-011-0041-6"},{"key":"14","doi-asserted-by":"crossref","unstructured":"14. Chopy, D., Pothlichet, J., Lafage, M., M\u00e9gret, F., Fiette, L., Si-Tahar, M. and Lafon, M. 2011. Ambivalent role of the innate immune response in rabies virus pathogenesis. <i>J. Virol.<\/i> 85: 6657\u20136668.","DOI":"10.1128\/JVI.00302-11"},{"key":"15","doi-asserted-by":"crossref","unstructured":"15. Dietzschold, B., Wunner, W. H., Wiktor, T. J., Lopes, A. D., Lafon, M., Smith, C. L. and Koprowski, H. 1983. Characterization of an antigenic determinant of the glycoprotein that correlates with pathogenicity of rabies virus. <i>Proc. Natl. Acad. Sci. U.S.A.<\/i> 80: 70\u201374.","DOI":"10.1073\/pnas.80.1.70"},{"key":"16","doi-asserted-by":"crossref","unstructured":"16. Faul, E. J., Wanjalla, C. N., Suthar, M. S., Gale, M., Wirblich, C. and Schnell, M. J. 2010. Rabies virus infection induces type I interferon production in an IPS-1 dependent manner while dendritic cell activation relies on IFNAR signaling. <i>PLoS Pathog.<\/i> 6: e1001016.","DOI":"10.1371\/journal.ppat.1001016"},{"key":"17","doi-asserted-by":"crossref","unstructured":"17. Fouquet, B., Nikolic, J., Larrous, F., Bourhy, H., Wirblich, C., Lagaudri\u00e8re-Gesbert, C. and Blondel, D. 2015. Focal adhesion kinase is involved in rabies virus infection through its interaction with viral phosphoprotein P. <i>J. Virol.<\/i> 89: 1640\u20131651.","DOI":"10.1128\/JVI.02602-14"},{"key":"18","doi-asserted-by":"crossref","unstructured":"18. Francis, J. R., Nourse, C., Vaska, V. L., Calvert, S., Northill, J. A., McCall, B. and Mattke, A. C. 2014. Australian Bat Lyssavirus in a child: the first reported case. <i>Pediatrics<\/i> 133: e1063\u2013e1067.","DOI":"10.1542\/peds.2013-1782"},{"key":"19","doi-asserted-by":"crossref","unstructured":"19. Gerard, F. C., Ribeiro, E. A. Jr., Leyrat, C., Ivanov, I., Blondel, D., Longhi, S., Ruigrok, R. W. and Jamin, M. 2009. Modular organization of rabies virus phosphoprotein. <i>J. Mol. Biol.<\/i> 388: 978\u2013996.","DOI":"10.1016\/j.jmb.2009.03.061"},{"key":"20","doi-asserted-by":"crossref","unstructured":"20. Hampson, K., Coudeville, L., Lembo, T., Sambo, M., Kieffer, A., Attlan, M., Barrat, J., Blanton, J. D., Briggs, D. J., Cleaveland, S., Costa, P., Freuling, C. M., Hiby, E., Knopf, L., Leanes, F., Meslin, F. X., Metlin, A., Miranda, M. E., M\u00fcller, T., Nel, L. H., Recuenco, S., Rupprecht, C. E., Schumacher, C., Taylor, L., Vigilato, M. A., Zinsstag, J., Dushoff, J., Global Alliance for Rabies Control Partners for Rabies Prevention 2015. Estimating the global burden of endemic canine rabies. <i>PLoS Negl. Trop. Dis.<\/i> 9: e0003709.","DOI":"10.1371\/journal.pntd.0003709"},{"key":"21","doi-asserted-by":"crossref","unstructured":"21. Hooper, D. C., Phares, T. W., Fabis, M. J. and Roy, A. 2009. The production of antibody by invading B cells is required for the clearance of rabies virus from the central nervous system. <i>PLoS Negl. Trop. Dis.<\/i> 3: e535.","DOI":"10.1371\/journal.pntd.0000535"},{"key":"22","doi-asserted-by":"crossref","unstructured":"22. Hornung, V., Ellegast, J., Kim, S., Brz\u00f3zka, K., Jung, A., Kato, H., Poeck, H., Akira, S., Conzelmann, K. K., Schlee, M., Endres, S. and Hartmann, G. 2006. 5\u2032-Triphosphate RNA is the ligand for RIG-I. <i>Science<\/i> 314: 994\u2013997.","DOI":"10.1126\/science.1132505"},{"key":"23","doi-asserted-by":"crossref","unstructured":"23. Ito, N., Moseley, G. W., Blondel, D., Shimizu, K., Rowe, C. L., Ito, Y., Masatani, T., Nakagawa, K., Jans, D. A. and Sugiyama, M. 2010. Role of interferon antagonist activity of rabies virus phosphoprotein in viral pathogenicity. <i>J. Virol.<\/i> 84: 6699\u20136710.","DOI":"10.1128\/JVI.00011-10"},{"key":"24","doi-asserted-by":"crossref","unstructured":"24. Ito, N., Mita, T., Shimizu, K., Ito, Y., Masatani, T., Nakagawa, K., Yamaoka, S., Abe, M., Okadera, K., Minamoto, N. and Sugiyama, M. 2011. Amino acid substitution at position 95 in rabies virus matrix protein affects viral pathogenicity. <i>J. Vet. Med. Sci.<\/i> 73: 1363\u20131366.","DOI":"10.1292\/jvms.11-0151"},{"key":"25","doi-asserted-by":"crossref","unstructured":"25. Jackson, A. C. 2013. Human Disease. pp. 269\u201398. <i>In<\/i>: Rabies, 3rd ed. (A. C. Jackson ed.), Academic Press, Oxford.","DOI":"10.1016\/B978-0-12-396547-9.00007-9"},{"key":"26","doi-asserted-by":"crossref","unstructured":"26. Jackson, A. C. and Fu, Z. F. 2013. Pathogenesis. pp. 299\u2013349. <i>In<\/i>: Rabies, 3rd ed. (A. C. Jackson ed.), Academic Press, Oxford.","DOI":"10.1016\/B978-0-12-396547-9.00008-0"},{"key":"27","doi-asserted-by":"crossref","unstructured":"27. Lafon, M. 2005. Modulation of the immune response in the nervous system by rabies virus. <i>Curr. Top. Microbiol. Immunol.<\/i> 289: 239\u2013258.","DOI":"10.1007\/3-540-27320-4_11"},{"key":"28","unstructured":"28. Lafon, M. 2008. Immune evasion, a critical strategy for rabies virus. <i>Dev. Biol. (Basel)<\/i> 131: 413\u2013419."},{"key":"29","doi-asserted-by":"crossref","unstructured":"29. Lafon, M. 2013. Immunology. pp. 387\u2013408. <i>In<\/i>: Rabies, 3rd. ed. (Jackson A. C. ed.), Academic Press, Oxford.","DOI":"10.1016\/B978-0-12-396547-9.00010-9"},{"key":"30","doi-asserted-by":"crossref","unstructured":"30. Lahaye, X., Vidy, A., Pomier, C., Obiang, L., Harper, F., Gaudin, Y. and Blondel, D. 2009. Functional characterization of Negri bodies (NBs) in rabies virus-infected cells: Evidence that NBs are sites of viral transcription and replication. <i>J. Virol.<\/i> 83: 7948\u20137958.","DOI":"10.1128\/JVI.00554-09"},{"key":"31","doi-asserted-by":"crossref","unstructured":"31. Leyrat, C., Ribeiro, E. A., Gerard, F. C. A., Ivanov, I., Ruigrok, R. W. H. and Jamin, M. 2011. Structure, interactions with host cell and functions of rhabdovirus phosphoprotein. <i>Future Virol.<\/i> 6: 465\u2013481.","DOI":"10.2217\/fvl.11.10"},{"key":"32","doi-asserted-by":"crossref","unstructured":"32. Li, Y., Dong, W., Shi, Y., Deng, F., Chen, X., Wan, C., Zhou, M., Zhao, L., Fu, Z. F. and Peng, G. 2016. Rabies virus phosphoprotein interacts with ribosomal protein L9 and affects rabies virus replication. <i>Virology<\/i> 488: 216\u2013224.","DOI":"10.1016\/j.virol.2015.11.018"},{"key":"33","doi-asserted-by":"crossref","unstructured":"33. Lieu, K. G., Brice, A., Wiltzer, L., Hirst, B., Jans, D. A., Blondel, D. and Moseley, G. W. 2013. The rabies virus interferon antagonist P protein interacts with activated STAT3 and inhibits Gp130 receptor signaling. <i>J. Virol.<\/i> 87: 8261\u20138265.","DOI":"10.1128\/JVI.00989-13"},{"key":"34","doi-asserted-by":"crossref","unstructured":"34. Luco, S., Delmas, O., Vidalain, P. O., Tangy, F., Weil, R. and Bourhy, H. 2012. RelAp43, a member of the NF-\u03baB family involved in innate immune response against Lyssavirus infection. <i>PLoS Pathog.<\/i> 8: e1003060.","DOI":"10.1371\/journal.ppat.1003060"},{"key":"35","doi-asserted-by":"crossref","unstructured":"35. Marschalek, A., Drechsel, L. and Conzelmann, K. K. 2012. The importance of being short: the role of rabies virus phosphoprotein isoforms assessed by differential IRES translation initiation. <i>Eur. J. Cell Biol.<\/i> 91: 17\u201323.","DOI":"10.1016\/j.ejcb.2011.01.009"},{"key":"36","doi-asserted-by":"crossref","unstructured":"36. Marschalek, A., Finke, S., Schwemmle, M., Mayer, D., Heimrich, B., Stitz, L. and Conzelmann, K. K. 2009. Attenuation of rabies virus replication and virulence by picornavirus internal ribosome entry site elements. <i>J. Virol.<\/i> 83: 1911\u20131919.","DOI":"10.1128\/JVI.02055-08"},{"key":"37","doi-asserted-by":"crossref","unstructured":"37. Masatani, T., Ito, N., Shimizu, K., Ito, Y., Nakagawa, K., Sawaki, Y., Koyama, H. and Sugiyama, M. 2010. Rabies virus nucleoprotein functions to evade activation of the RIG-I-mediated antiviral response. <i>J. Virol.<\/i> 84: 4002\u20134012.","DOI":"10.1128\/JVI.02220-09"},{"key":"38","doi-asserted-by":"crossref","unstructured":"38. Masatani, T., Ito, N., Shimizu, K., Ito, Y., Nakagawa, K., Abe, M., Yamaoka, S. and Sugiyama, M. 2011. Amino acids at positions 273 and 394 in rabies virus nucleoprotein are important for both evasion of host RIG-I-mediated antiviral response and pathogenicity. <i>Virus Res.<\/i> 155: 168\u2013174.","DOI":"10.1016\/j.virusres.2010.09.016"},{"key":"39","doi-asserted-by":"crossref","unstructured":"39. Masatani, T., Ito, N., Ito, Y., Nakagawa, K., Abe, M., Yamaoka, S., Okadera, K. and Sugiyama, M. 2013. Importance of rabies virus nucleoprotein in viral evasion of interferon response in the brain. <i>Microbiol. Immunol.<\/i> 57: 511\u2013517.","DOI":"10.1111\/1348-0421.12058"},{"key":"40","doi-asserted-by":"crossref","unstructured":"41. M\u00e9gret, F., Prehaud, C., Lafage, M., Moreau, P., Rouas-Freiss, N., Carosella, E. D. and Lafon, M. 2007. Modulation of HLA-G and HLA-E expression in human neuronal cells after rabies virus or herpes virus simplex type 1 infections. <i>Hum. Immunol.<\/i> 68: 294\u2013302.","DOI":"10.1016\/j.humimm.2006.12.003"},{"key":"41","doi-asserted-by":"crossref","unstructured":"42. M\u00e9nager, P., Roux, P., M\u00e9gret, F., Bourgeois, J. P., Le Sourd, A. M., Danckaert, A., Lafage, M., Pr\u00e9haud, C. and Lafon, M. 2009. Toll-like receptor 3 (TLR3) plays a major role in the formation of rabies virus Negri Bodies. <i>PLoS Pathog.<\/i> 5: e1000315.","DOI":"10.1371\/journal.ppat.1000315"},{"key":"42","doi-asserted-by":"crossref","unstructured":"43. Morimoto, K., Hooper, D. C., Spitsin, S., Koprowski, H. and Dietzschold, B. 1999. Pathogenicity of different rabies virus variants inversely correlates with apoptosis and rabies virus glycoprotein expression in infected primary neuron cultures. <i>J. Virol.<\/i> 73: 510\u2013518.","DOI":"10.1128\/JVI.73.1.510-518.1999"},{"key":"43","doi-asserted-by":"crossref","unstructured":"44. Moseley, G. W. 2012. Viral Interferon Antagonism: Making the Leap from the Bench to the Clinic. <i>J. Virol. Antivir. Res.<\/i> 1: 1\u20132.","DOI":"10.4172\/2324-8955.1000e103"},{"key":"44","doi-asserted-by":"crossref","unstructured":"45. Moseley, G. W., Filmer, R. P., DeJesus, M. A. and Jans, D. A. 2007. Nucleocytoplasmic distribution of rabies virus P-protein is regulated by phosphorylation adjacent to C-terminal nuclear import and export signals. <i>Biochemistry<\/i> 46: 12053\u201312061.","DOI":"10.1021\/bi700521m"},{"key":"45","doi-asserted-by":"crossref","unstructured":"46. Moseley, G. W., Roth, D. M., DeJesus, M. A., Leyton, D. L., Filmer, R. P., Pouton, C. W. and Jans, D. A. 2007. Dynein light chain association sequences can facilitate nuclear protein import. <i>Mol. Biol. Cell<\/i> 18: 3204\u20133213.","DOI":"10.1091\/mbc.E07-01-0030"},{"key":"46","doi-asserted-by":"crossref","unstructured":"47. Moseley, G. W., Lahaye, X., Roth, D. M., Oksayan, S., Filmer, R. P., Rowe, C. L., Blondel, D. and Jans, D. A. 2009. Dual modes of rabies P-protein association with microtubules: a novel strategy to suppress the antiviral response. <i>J. Cell Sci.<\/i> 122: 3652\u20133662.","DOI":"10.1242\/jcs.045542"},{"key":"47","doi-asserted-by":"crossref","unstructured":"48. Niu, X., Tang, L., Tseggai, T., Guo, Y. and Fu, Z. F. 2013. Wild-type rabies virus phosphoprotein is associated with viral sensitivity to type I interferon treatment. <i>Arch. Virol.<\/i> 158: 2297\u20132305.","DOI":"10.1007\/s00705-013-1743-2"},{"key":"48","doi-asserted-by":"crossref","unstructured":"49. Oksayan, S., Ito, N., Moseley, G. and Blondel, D. 2012. Subcellular trafficking in rhabdovirus infection and immune evasion: a novel target for therapeutics. <i>Infect. Disord. Drug Targets<\/i> 12: 38\u201358.","DOI":"10.2174\/187152612798994966"},{"key":"49","doi-asserted-by":"crossref","unstructured":"50. Oksayan, S., Wiltzer, L., Rowe, C. L., Blondel, D., Jans, D. A. and Moseley, G. W. 2012. A novel nuclear trafficking module regulates the nucleocytoplasmic localization of the rabies virus interferon antagonist, P protein. <i>J. Biol. Chem.<\/i> 287: 28112\u201328121.","DOI":"10.1074\/jbc.M112.374694"},{"key":"50","doi-asserted-by":"crossref","unstructured":"51. Oksayan, S., Nikolic, J., David, C. T., Blondel, D., Jans, D. A. and Moseley, G. W. 2015. Identification of a role for nucleolin in rabies virus infection. <i>J. Virol.<\/i> 89: 1939\u20131943.","DOI":"10.1128\/JVI.03320-14"},{"key":"51","doi-asserted-by":"crossref","unstructured":"52. Pasdeloup, D., Poisson, N., Raux, H., Gaudin, Y., Ruigrok, R. W. and Blondel, D. 2005. Nucleocytoplasmic shuttling of the rabies virus P protein requires a nuclear localization signal and a CRM1-dependent nuclear export signal. <i>Virology<\/i> 334: 284\u2013293.","DOI":"10.1016\/j.virol.2005.02.005"},{"key":"52","doi-asserted-by":"crossref","unstructured":"53. Phares, T. W., Kean, R. B., Mikheeva, T. and Hooper, D. C. 2006. Regional differences in blood-brain barrier permeability changes and inflammation in the apathogenic clearance of virus from the central nervous system. <i>J. Immunol.<\/i> 176: 7666\u20137675.","DOI":"10.4049\/jimmunol.176.12.7666"},{"key":"53","doi-asserted-by":"crossref","unstructured":"54. Phares, T. W., Fabis, M. J., Brimer, C. M., Kean, R. B. and Hooper, D. C. 2007. A peroxynitrite-dependent pathway is responsible for blood-brain barrier permeability changes during a central nervous system inflammatory response: TNF-alpha is neither necessary nor sufficient. <i>J. Immunol.<\/i> 178: 7334\u20137343.","DOI":"10.4049\/jimmunol.178.11.7334"},{"key":"54","doi-asserted-by":"crossref","unstructured":"55. Randall, R. E. and Goodbourn, S. 2008. Interferons and viruses: an interplay between induction, signalling, antiviral responses and virus countermeasures. <i>J. Gen. Virol.<\/i> 89: 1\u201347.","DOI":"10.1099\/vir.0.83391-0"},{"key":"55","doi-asserted-by":"crossref","unstructured":"56. Rawlinson, S. M. and Moseley, G. W. 2015. The nucleolar interface of RNA viruses. <i>Cell. Microbiol.<\/i> 17: 1108\u20131120.","DOI":"10.1111\/cmi.12465"},{"key":"56","doi-asserted-by":"crossref","unstructured":"57. Ribeiro, E. A. Jr., Leyrat, C., G\u00e9rard, F. C. A., Albertini, A. A. V., Falk, C., Ruigrok, R. W. H. and Jamin, M. 2009. Binding of rabies virus polymerase cofactor to recombinant circular nucleoprotein-RNA complexes. <i>J. Mol. Biol.<\/i> 394: 558\u2013575.","DOI":"10.1016\/j.jmb.2009.09.042"},{"key":"57","doi-asserted-by":"crossref","unstructured":"58. Rieder, M., Brz\u00f3zka, K., Pfaller, C. K., Cox, J. H., Stitz, L. and Conzelmann, K. K. 2011. Genetic dissection of interferon-antagonistic functions of rabies virus phosphoprotein: inhibition of interferon regulatory factor 3 activation is important for pathogenicity. <i>J. Virol.<\/i> 85: 842\u2013852.","DOI":"10.1128\/JVI.01427-10"},{"key":"58","doi-asserted-by":"crossref","unstructured":"59. Rossiter, J. P. and Jackson, A. C. 2013. Pathology. pp. 351\u2013386. <i>In<\/i>: Rabies, 3rd ed. (Jackson A. C. ed.), Academic Press, Oxford.","DOI":"10.1016\/B978-0-12-396547-9.00009-2"},{"key":"59","doi-asserted-by":"crossref","unstructured":"60. Rowe, C. L., Wagstaff, K. M., Oksayan, S., Glover, D. J., Jans, D. A. and Moseley, G. W. 2016. Nuclear Trafficking of the Rabies Virus Interferon Antagonist P-Protein Is Regulated by an Importin-Binding Nuclear Localization Sequence in the C-Terminal Domain. <i>PLoS ONE<\/i> 11: e0150477.","DOI":"10.1371\/journal.pone.0150477"},{"key":"60","doi-asserted-by":"crossref","unstructured":"61. Roy, A. and Hooper, D. C. 2007. Lethal silver-haired bat rabies virus infection can be prevented by opening the blood-brain barrier. <i>J. Virol.<\/i> 81: 7993\u20137998.","DOI":"10.1128\/JVI.00710-07"},{"key":"61","doi-asserted-by":"crossref","unstructured":"62. Roy, A., Phares, T. W., Koprowski, H. and Hooper, D. C. 2007. Failure to open the blood-brain barrier and deliver immune effectors to central nervous system tissues leads to the lethal outcome of silver-haired bat rabies virus infection. <i>J. Virol.<\/i> 81: 1110\u20131118.","DOI":"10.1128\/JVI.01964-06"},{"key":"62","doi-asserted-by":"crossref","unstructured":"63. Sadler, A. J. and Williams, B. R. 2008. Interferon-inducible antiviral effectors. <i>Nat. Rev. Immunol.<\/i> 8: 559\u2013568.","DOI":"10.1038\/nri2314"},{"key":"63","doi-asserted-by":"crossref","unstructured":"64. Schindler, C., Levy, D. E. and Decker, T. 2007. JAK-STAT signaling: from interferons to cytokines. <i>J. Biol. Chem.<\/i> 282: 20059\u201320063.","DOI":"10.1074\/jbc.R700016200"},{"key":"64","doi-asserted-by":"crossref","unstructured":"65. Schnell, M. J., McGettigan, J. P., Wirblich, C. and Papaneri, A. 2010. The cell biology of rabies virus: using stealth to reach the brain. <i>Nat. Rev. Microbiol.<\/i> 8: 51\u201361.","DOI":"10.1038\/nrmicro2260"},{"key":"65","doi-asserted-by":"crossref","unstructured":"66. Shaw, M. L., Cardenas, W. B., Zamarin, D., Palese, P. and Basler, C. F. 2005. Nuclear localization of the Nipah virus W protein allows for inhibition of both virus- and toll-like receptor 3-triggered signaling pathways. <i>J. Virol.<\/i> 79: 6078\u20136088.","DOI":"10.1128\/JVI.79.10.6078-6088.2005"},{"key":"66","doi-asserted-by":"crossref","unstructured":"67. Shimizu, K., Ito, N., Mita, T., Yamada, K., Hosokawa-Muto, J., Sugiyama, M. and Minamoto, N. 2007. Involvement of nucleoprotein, phosphoprotein, and matrix protein genes of rabies virus in virulence for adult mice. <i>Virus Res.<\/i> 123: 154\u2013160.","DOI":"10.1016\/j.virusres.2006.08.011"},{"key":"67","doi-asserted-by":"crossref","unstructured":"68. Takayama-Ito, M., Ito, N., Yamada, K., Sugiyama, M. and Minamoto, N. 2006. Multiple amino acids in the glycoprotein of rabies virus are responsible for pathogenicity in adult mice. <i>Virus Res.<\/i> 115: 169\u2013175.","DOI":"10.1016\/j.virusres.2005.08.004"},{"key":"68","doi-asserted-by":"crossref","unstructured":"69. Tuffereau, C., Leblois, H., B\u00e9n\u00e9jean, J., Coulon, P., Lafay, F. and Flamand, A. 1989. Arginine or lysine in position 333 of ERA and CVS glycoprotein is necessary for rabies virulence in adult mice. <i>Virology<\/i> 172: 206\u2013212.","DOI":"10.1016\/0042-6822(89)90122-0"},{"key":"69","doi-asserted-by":"crossref","unstructured":"70. Versteeg, G. A. and Garc\u00eda-Sastre, A. 2010. Viral tricks to grid-lock the type I interferon system. <i>Curr. Opin. Microbiol.<\/i> 13: 508\u2013516.","DOI":"10.1016\/j.mib.2010.05.009"},{"key":"70","doi-asserted-by":"crossref","unstructured":"71. Vidy, A., Chelbi-Alix, M. and Blondel, D. 2005. Rabies virus P protein interacts with STAT1 and inhibits interferon signal transduction pathways. <i>J. Virol.<\/i> 79: 14411\u201314420.","DOI":"10.1128\/JVI.79.22.14411-14420.2005"},{"key":"71","doi-asserted-by":"crossref","unstructured":"72. Vidy, A., El Bougrini, J., Chelbi-Alix, M. K. and Blondel, D. 2007. The nucleocytoplasmic rabies virus P protein counteracts interferon signaling by inhibiting both nuclear accumulation and DNA binding of STAT1. <i>J. Virol.<\/i> 81: 4255\u20134263.","DOI":"10.1128\/JVI.01930-06"},{"key":"72","doi-asserted-by":"crossref","unstructured":"73. Vos, A., Conzelmann, K. K., Finke, S., M\u00fcller, T., Teifke, J., Fooks, A. R. and Neubert, A. 2011. Immunogenicity studies in carnivores using a rabies virus construct with a site-directed deletion in the phosphoprotein. <i>Adv. Prev. Med.<\/i> 2011: 898171.","DOI":"10.4061\/2011\/898171"},{"key":"73","doi-asserted-by":"crossref","unstructured":"74. Wang, Z. W., Sarmento, L., Wang, Y., Li, X. Q., Dhingra, V., Tseggai, T., Jiang, B. and Fu, Z. F. 2005. Attenuated rabies virus activates, while pathogenic rabies virus evades, the host innate immune responses in the central nervous system. <i>J. Virol.<\/i> 79: 12554\u201312565.","DOI":"10.1128\/JVI.79.19.12554-12565.2005"},{"key":"74","doi-asserted-by":"crossref","unstructured":"75. Wiltzer, L., Larrous, F., Oksayan, S., Ito, N., Marsh, G. A., Wang, L. F., Blondel, D., Bourhy, H., Jans, D. A. and Moseley, G. W. 2012. Conservation of a unique mechanism of immune evasion across the Lyssavirus genus. <i>J. Virol.<\/i> 86: 10194\u201310199.","DOI":"10.1128\/JVI.01249-12"},{"key":"75","doi-asserted-by":"crossref","unstructured":"76. Wiltzer, L., Okada, K., Yamaoka, S., Larrous, F., Kuusisto, H. V., Sugiyama, M., Blondel, D., Bourhy, H., Jans, D. A., Ito, N. and Moseley, G. W. 2014. Interaction of rabies virus P-protein with STAT proteins is critical to lethal rabies disease. <i>J. Infect. Dis.<\/i> 209: 1744\u20131753.","DOI":"10.1093\/infdis\/jit829"},{"key":"76","unstructured":"77. World Health Organization 2013. WHO Expert Consultation on Rabies. Second report. <i>World Health Organ. Tech. Rep. Ser.<\/i> 982: 1\u2013139 back cover."},{"key":"77","doi-asserted-by":"crossref","unstructured":"78. Yamaoka, S., Ito, N., Ohka, S., Kaneda, S., Nakamura, H., Agari, T., Masatani, T., Nakagawa, K., Okada, K., Okadera, K., Mitake, H., Fujii, T. and Sugiyama, M. 2013. Involvement of the rabies virus phosphoprotein gene in neuroinvasiveness. <i>J. Virol.<\/i> 87: 12327\u201312338.","DOI":"10.1128\/JVI.02132-13"}],"container-title":["Journal of Veterinary Medical Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/jvms\/78\/7\/78_16-0092\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,9,18]],"date-time":"2020-09-18T02:38:42Z","timestamp":1600396722000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/jvms\/78\/7\/78_16-0092\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016]]},"references-count":77,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2016]]}},"URL":"https:\/\/doi.org\/10.1292\/jvms.16-0092","relation":{},"ISSN":["0916-7250","1347-7439"],"issn-type":[{"value":"0916-7250","type":"print"},{"value":"1347-7439","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016]]}}}