dc.contributor.authorTo, Janet
dc.contributor.authorSurya, Wahyu
dc.contributor.authorFung, To Sing
dc.contributor.authorLi, Yan
dc.contributor.authorVerdià-Bàguena, Carmina
dc.contributor.authorQueralt-Martin, Maria
dc.contributor.authorAguilella, Vicente M.
dc.contributor.authorLiu, Ding Xiang
dc.contributor.authorTorres, Jaume
dc.contributor.editorPerlman, Stanley*
dc.date.accessioned2017-06-20T06:39:28Z
dc.date.available2017-06-20T06:39:28Z
dc.date.issued2017
dc.identifier.citationTo, J., Surya, W., Fung, T. S., Li, Y., Verdià-Bàguena, C., Queralt-Martin, M., et al. (2017). Channel-Inactivating Mutations and Their Revertant Mutants in the Envelope Protein of Infectious Bronchitis Virus. Journal of Virology, 91(5), e02158-16-.en_US
dc.identifier.issn0022-538Xen_US
dc.identifier.urihttp://hdl.handle.net/10220/42733
dc.description.abstractIt has been shown previously in the severe acute respiratory syndrome coronavirus (SARS-CoV) that two point mutations, N15A and V25F, in the transmembrane domain (TMD) of the envelope (E) protein abolished channel activity and led to in vivo attenuation. Pathogenicity was recovered in mutants that also regained E protein channel activity. In particular, V25F was rapidly compensated by changes at multiple V25F-facing TMD residues located on a neighboring monomer, consistent with a recovery of oligomerization. Here, we show using infected cells that the same mutations, T16A and A26F, in the gamma-CoV infectious bronchitis virus (IBV) lead to, in principle, similar results. However, IBV E A26F did not abolish oligomer formation and was compensated by mutations at N- and C-terminal extramembrane domains (EMDs). The C-terminal EMD mutations clustered along an insertion sequence specific to gamma-CoVs. Nuclear magnetic resonance data are consistent with the presence of only one TMD in IBV E, suggesting that recovery of channel activity and fitness in these IBV E revertant mutants is through an allosteric interaction between EMDs and TMD. The present results are important for the development of IBV live attenuated vaccines when channel-inactivating mutations are introduced in the E protein.en_US
dc.format.extent20 p.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesJournal of Virologyen_US
dc.rights© 2017 American Society for Microbiology (ASM). This paper was published in Journal of Virology and is made available as an electronic reprint (preprint) with permission of American Society for Microbiology (ASM). The published version is available at: [http://dx.doi.org/10.1128/JVI.02158-16]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.en_US
dc.subjectCoronavirusen_US
dc.subjectInfectious bronchitis virusen_US
dc.titleChannel-Inactivating Mutations and Their Revertant Mutants in the Envelope Protein of Infectious Bronchitis Virusen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1128/JVI.02158-16
dc.description.versionPublished versionen_US


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