Structural insight into African horsesickness virus infection

 

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dc.contributor.author Manole, V
dc.contributor.author Laurinmäki, P
dc.contributor.author van Wyngaardt, W
dc.contributor.author Potgieter, C A
dc.contributor.author Wright, I M
dc.contributor.author Venter, G J
dc.contributor.author van Dijk, A A
dc.contributor.author Sewell, B T
dc.contributor.author Butcher, S J
dc.date.accessioned 2016-07-26T08:54:10Z
dc.date.available 2016-07-26T08:54:10Z
dc.date.issued 2012
dc.identifier http://dx.doi.org/10.1128/JVI.00517-12
dc.identifier.citation Manole, 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.issn 0022-538X en_ZA
dc.identifier.uri http://hdl.handle.net/11427/20743
dc.description.abstract 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. en_ZA
dc.language.iso eng
dc.publisher American Society for Microbiology en_ZA
dc.source Journal of Virology en_ZA
dc.source.uri http://jvi.asm.org/
dc.title Structural insight into African horsesickness virus infection en_ZA
dc.type Journal Article en_ZA
dc.date.updated 2016-07-14T17:55:08Z
uct.type.publication Research en_ZA
uct.type.resource Article en_ZA
dc.publisher.institution University of Cape Town
uct.type.filetype Text
uct.type.filetype Image
dc.identifier.apacitation Manole, 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/11427/20743 en_ZA
dc.identifier.chicagocitation Manole, 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/11427/20743 en_ZA
dc.identifier.vancouvercitation Manole 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.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


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