Orsay Virus CP-δ Adopts a Novel β-Bracelet Structural Fold and Incorporates into Virions as a Head Fiber

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dc.citation.articleNumbere01560-20en_US
dc.citation.issueNumber21en_US
dc.citation.journalTitleJournal of Virologyen_US
dc.citation.volumeNumber94en_US
dc.contributor.authorGuo, Yusong R.en_US
dc.contributor.authorFan, Yanlinen_US
dc.contributor.authorZhou, Yingen_US
dc.contributor.authorJin, Miaoen_US
dc.contributor.authorZhang, Jim L.en_US
dc.contributor.authorJiang, Hongbingen_US
dc.contributor.authorHolt, Matthew V.en_US
dc.contributor.authorWang, Taoen_US
dc.contributor.authorYoung, Nicolas L.en_US
dc.contributor.authorWang, Daviden_US
dc.contributor.authorZhong, Weiweien_US
dc.contributor.authorTao, Yizhi Janeen_US
dc.date.accessioned2020-11-11T20:20:28Zen_US
dc.date.available2020-11-11T20:20:28Zen_US
dc.date.issued2020en_US
dc.description.abstractFiber proteins are commonly found in eukaryotic and prokaryotic viruses, where they play important roles in mediating viral attachment and host cell entry. They typically form trimeric structures and are incorporated into virions via noncovalent interactions. Orsay virus, a small RNA virus which specifically infects the laboratory model nematode Caenorhabditis elegans, encodes a fibrous protein δ that can be expressed as a free protein and as a capsid protein-δ (CP-δ) fusion protein. Free δ has previously been demonstrated to facilitate viral exit following intracellular expression; however, the biological significance and prevalence of CP-δ remained relatively unknown. Here, we demonstrate that Orsay CP-δ is covalently incorporated into infectious particles, the first example of any attached viral fibers known to date. The crystal structure of δ(1–101) (a deletion mutant containing the first 101 amino acid [aa] residues of δ) reveals a pentameric, 145-Å long fiber with an N-terminal coiled coil followed by multiple β-bracelet repeats. Electron micrographs of infectious virions depict particle-associated CP-δ fibers with dimensions similar to free δ. The δ proteins from two other nematode viruses, Le Blanc and Santeuil, which both specifically infect Caenorhabditis briggsae, were also found to form fibrous molecules. Recombinant Le Blanc δ was able to block Orsay virus infection in worm culture and vice versa, suggesting these two viruses likely compete for the same cell receptor(s). Thus, we propose that while CP-δ likely mediates host cell attachment for all three nematode viruses, additional downstream factor(s) ultimately determine the host specificity and range of each virus.en_US
dc.identifier.citationGuo, Yusong R., Fan, Yanlin, Zhou, Ying, et al.. "Orsay Virus CP-δ Adopts a Novel β-Bracelet Structural Fold and Incorporates into Virions as a Head Fiber." <i>Journal of Virology,</i> 94, no. 21 (2020) American Society for Microbiology: https://doi.org/10.1128/JVI.01560-20.en_US
dc.identifier.doihttps://doi.org/10.1128/JVI.01560-20en_US
dc.identifier.urihttps://hdl.handle.net/1911/109550en_US
dc.language.isoengen_US
dc.publisherAmerican Society for Microbiologyen_US
dc.rightsThis is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en_US
dc.subject.keywordOrsay virusen_US
dc.subject.keywordcrystallographyen_US
dc.subject.keywordCaenorhabditis elegansen_US
dc.subject.keywordβ-braceleten_US
dc.subject.keywordviral fiberen_US
dc.titleOrsay Virus CP-δ Adopts a Novel β-Bracelet Structural Fold and Incorporates into Virions as a Head Fiberen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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