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Structure of a pentameric virion-associated fiber with a potential role in Orsay virus entry to host cells

PLoS pathogens, 2017-02, Vol.13 (2), p.e1006231 [Peer Reviewed Journal]

COPYRIGHT 2017 Public Library of Science ;COPYRIGHT 2017 Public Library of Science ;2017 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Fan Y, Guo YR, Yuan W, Zhou Y, Holt MV, Wang T, et al. (2017) Structure of a pentameric virion-associated fiber with a potential role in Orsay virus entry to host cells. PLoS Pathog 13(2): e1006231. doi:10.1371/journal.ppat.1006231 ;2017 Fan et al 2017 Fan et al ;2017 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Fan Y, Guo YR, Yuan W, Zhou Y, Holt MV, Wang T, et al. (2017) Structure of a pentameric virion-associated fiber with a potential role in Orsay virus entry to host cells. PLoS Pathog 13(2): e1006231. doi:10.1371/journal.ppat.1006231 ;ISSN: 1553-7374 ;ISSN: 1553-7366 ;EISSN: 1553-7374 ;DOI: 10.1371/journal.ppat.1006231 ;PMID: 28241071

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Title:
Structure of a pentameric virion-associated fiber with a potential role in Orsay virus entry to host cells
Author: Fan, Yanlin ; Guo, Yusong R ; Yuan, Wang ; Zhou, Ying ; Holt, Matthew V ; Wang, Tao ; Demeler, Borries ; Young, Nicolas L ; Zhong, Weiwei ; Tao, Yizhi J
Rey, Félix A.
Subjects: Adenoviridae ; Animals ; BASIC BIOLOGICAL SCIENCES ; Biology and Life Sciences ; Caenorhabditis elegans ; Caenorhabditis elegans - virology ; Capsid Proteins - chemistry ; Capsid Proteins - ultrastructure ; Circular Dichroism ; Colleges & universities ; Crystal structure ; Crystallography, X-Ray ; Genes ; Host-virus relationships ; Mass Spectrometry ; Medicine and Health Sciences ; Microscopy, Electron, Transmission ; Mutagenesis, Site-Directed ; Nematoda ; Nematode infections ; Nematodes ; Organisms, Genetically Modified ; Physical Sciences ; Protein structure ; Proteins ; Recombinant proteins ; Reoviridae ; Research and Analysis Methods ; RNA interference ; RNA Virus Infections ; RNA viruses ; RNA Viruses - physiology ; RNA Viruses - ultrastructure ; Structure ; Testing ; Viral packaging ; Viral structure ; Virion - chemistry ; Virion - ultrastructure ; Virulence (Microbiology) ; Virus Internalization ; Viruses
Is Part Of: PLoS pathogens, 2017-02, Vol.13 (2), p.e1006231
Description: 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.
Publisher: United States: Public Library of Science
Language: English
Identifier: ISSN: 1553-7374
ISSN: 1553-7366
EISSN: 1553-7374
DOI: 10.1371/journal.ppat.1006231
PMID: 28241071
Source: PLoS OA刊
DOAJ Directory of Open Access Journals
Geneva Foundation Free Medical Journals at publisher websites
MEDLINE
PubMed Central
Coronavirus Research Database
ProQuest Central

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Structure of a pentameric virion-associated fiber with a potential role in Orsay virus entry to host cells

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