Structural insight into African horsesickness virus infection

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dc.contributor.authorManole, V
dc.contributor.authorLaurinmäki, P
dc.contributor.authorvan Wyngaardt, W
dc.contributor.authorPotgieter, C A
dc.contributor.authorWright, I M
dc.contributor.authorVenter, G J
dc.contributor.authorvan Dijk, A A
dc.contributor.authorSewell, B T
dc.contributor.authorButcher, S J
dc.date.accessioned2016-07-26T08:54:10Z
dc.date.available2016-07-26T08:54:10Z
dc.date.issued2012
dc.date.updated2016-07-14T17:55:08Z
dc.description.abstractAfrican horsesickness (AHS) is a devastating disease of horses. The disease is caused by the double-stranded RNA-containing African horsesickness virus (AHSV). Using electron cryomicroscopy and three-dimensional image reconstruction, we determined the architecture of an AHSV serotype 4 (AHSV-4) reference strain. The structure revealed triple-layered AHS virions enclosing the segmented genome and transcriptase complex. The innermost protein layer contains 120 copies of VP3, with the viral polymerase, capping enzyme, and helicase attached to the inner surface of the VP3 layer on the 5-fold axis, surrounded by double-stranded RNA. VP7 trimers form a second, T 13 layer on top of VP3. Comparative analyses of the structures of bluetongue virus and AHSV-4 confirmed that VP5 trimers form globular domains and VP2 trimers form triskelions, on the virion surface. We also identified an AHSV-7 strain with a truncated VP2 protein (AHSV-7 tVP2) which outgrows AHSV-4 in culture. Comparison of AHSV-7 tVP2 to bluetongue virus and AHSV-4 allowed mapping of two domains in AHSV-4 VP2, and one in bluetongue virus VP2, that are important in infection. We also revealed a protein plugging the 5-fold vertices in AHSV-4. These results shed light on virus-host interactions in an economically important orbivirus to help the informed design of new vaccines.en_ZA
dc.identifierhttp://dx.doi.org/10.1128/JVI.00517-12
dc.identifier.apacitationManole, V., Laurinmäki, P., van Wyngaardt, W., Potgieter, C. A., Wright, I. M., Venter, G. J., ... Butcher, S. J. (2012). Structural insight into African horsesickness virus infection. <i>Journal of Virology</i>, http://hdl.handle.net/11427/20743en_ZA
dc.identifier.chicagocitationManole, V, P Laurinmäki, W van Wyngaardt, C A Potgieter, I M Wright, G J Venter, A A van Dijk, B T Sewell, and S J Butcher "Structural insight into African horsesickness virus infection." <i>Journal of Virology</i> (2012) http://hdl.handle.net/11427/20743en_ZA
dc.identifier.citationManole, V., Laurinmäki, P., Van Wyngaardt, W., Potgieter, C. A., Wright, I. M., Venter, G. J., ... & Butcher, S. J. (2012). Structural insight into African horsesickness virus infection. Journal of virology, 86(15), 7858-7866.en_ZA
dc.identifier.issn0022-538Xen_ZA
dc.identifier.ris TY - Journal Article AU - Manole, V AU - Laurinmäki, P AU - van Wyngaardt, W AU - Potgieter, C A AU - Wright, I M AU - Venter, G J AU - van Dijk, A A AU - Sewell, B T AU - Butcher, S J AB - African horsesickness (AHS) is a devastating disease of horses. The disease is caused by the double-stranded RNA-containing African horsesickness virus (AHSV). Using electron cryomicroscopy and three-dimensional image reconstruction, we determined the architecture of an AHSV serotype 4 (AHSV-4) reference strain. The structure revealed triple-layered AHS virions enclosing the segmented genome and transcriptase complex. The innermost protein layer contains 120 copies of VP3, with the viral polymerase, capping enzyme, and helicase attached to the inner surface of the VP3 layer on the 5-fold axis, surrounded by double-stranded RNA. VP7 trimers form a second, T 13 layer on top of VP3. Comparative analyses of the structures of bluetongue virus and AHSV-4 confirmed that VP5 trimers form globular domains and VP2 trimers form triskelions, on the virion surface. We also identified an AHSV-7 strain with a truncated VP2 protein (AHSV-7 tVP2) which outgrows AHSV-4 in culture. Comparison of AHSV-7 tVP2 to bluetongue virus and AHSV-4 allowed mapping of two domains in AHSV-4 VP2, and one in bluetongue virus VP2, that are important in infection. We also revealed a protein plugging the 5-fold vertices in AHSV-4. These results shed light on virus-host interactions in an economically important orbivirus to help the informed design of new vaccines. DA - 2012 DB - OpenUCT DP - University of Cape Town J1 - Journal of Virology LK - https://open.uct.ac.za PB - University of Cape Town PY - 2012 SM - 0022-538X T1 - Structural insight into African horsesickness virus infection TI - Structural insight into African horsesickness virus infection UR - http://hdl.handle.net/11427/20743 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/20743
dc.identifier.vancouvercitationManole V, Laurinmäki P, van Wyngaardt W, Potgieter CA, Wright IM, Venter GJ, et al. Structural insight into African horsesickness virus infection. Journal of Virology. 2012; http://hdl.handle.net/11427/20743.en_ZA
dc.language.isoeng
dc.publisherAmerican Society for Microbiologyen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.sourceJournal of Virologyen_ZA
dc.source.urihttp://jvi.asm.org/
dc.titleStructural insight into African horsesickness virus infectionen_ZA
dc.typeJournal Articleen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceArticleen_ZA
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