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dc.contributor.author Fan, Yanlin
dc.contributor.author Guo, Yusong R.
dc.contributor.author Yuan, Wang
dc.contributor.author Zhou, Ying
dc.contributor.author Holt, Matthew V.
dc.contributor.author Wang, Tao
dc.contributor.author Demeler, Borries
dc.contributor.author Young, Nicolas L.
dc.contributor.author Zhong, Weiwei
dc.contributor.author Tao, Yizhi J.
dc.date.accessioned 2021-07-14T00:53:46Z
dc.date.available 2021-07-14T00:53:46Z
dc.date.issued 2017
dc.identifier.citation Fan, Y., Guo, Y. R., Yuan, W., Zhou, Y., Holt, M. V., Wang, T., Demeler, B., Young, N. L., Zhong, W., & Tao, Y. J. (2017). Structure of a pentameric virion-associated fiber with a potential role in Orsay virus entry to host cells. PLoS Pathogens, 13(2), Article e1006231. https://doi.org/10.1371/journal.ppat.1006231 en_US
dc.identifier.uri https://hdl.handle.net/10133/5956
dc.description Open access article. Creative Commons Attribution 4.0 International License (CC BY 4.0) applies en_US
dc.description.abstract Despite the wide use of Caenorhabditis elegans as a model organism, the first virus naturally infecting this organism was not discovered until six years ago. The Orsay virus and its related nematode viruses have a positive-sense RNA genome, encoding three proteins: CP, RdRP, and a novel δ protein that shares no homology with any other proteins. δ can be expressed either as a free δ or a CP-δ fusion protein by ribosomal frameshift, but the structure and function of both δ and CP-δ remain unknown. Using a combination of electron microscopy, X-ray crystallography, computational and biophysical analyses, here we show that the Orsay δ protein forms a ~420-Å long, pentameric fiber with an N-terminal α-helical bundle, a β-stranded filament in the middle, and a C-terminal head domain. The pentameric nature of the δ fiber has been independently confirmed by both mass spectrometry and analytical ultracentrifugation. Recombinant Orsay capsid containing CP-δ shows protruding long fibers with globular heads at the distal end. Mutant viruses with disrupted CP-δ fibers were generated by organism-based reverse genetics. These viruses were found to be either non-viable or with poor infectivity according to phenotypic and qRT-PCR analyses. Furthermore, addition of purified δ proteins to worm culture greatly reduced Orsay infectivity in a sequence-specific manner. Based on the structure resemblance between the Orsay CP-δ fiber and the fibers from reovirus and adenovirus, we propose that CP-δ functions as a cell attachment protein to mediate Orsay entry into worm intestine cells. en_US
dc.language.iso en_US en_US
dc.publisher Public Library of Science en_US
dc.subject Orsay en_US
dc.subject Crystal structure en_US
dc.subject Pentameric en_US
dc.title Structure of pentameric virion-associated fiber with a potential role in Orsay virus entry to host cells en_US
dc.type Article en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.description.peer-review Yes en_US
dc.publisher.institution Rice University en_US
dc.publisher.institution Baylor College of Medicine en_US
dc.publisher.institution University of Texas Health Science Center at San Antonio en_US
dc.publisher.institution University of Lethbridge en_US
dc.publisher.url https://doi.org/10.1371/journal.ppat.1006231 en_US


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