Reovirus σ1 Conformational Flexibility Modulates the Efficiency of Host Cell Attachment.
crosslink
disulfide
glycan
junctional adhesion molecule-A
receptor
reovirus
sialic acid
Journal
Journal of virology
ISSN: 1098-5514
Titre abrégé: J Virol
Pays: United States
ID NLM: 0113724
Informations de publication
Date de publication:
09 11 2020
09 11 2020
Historique:
received:
09
06
2020
accepted:
09
09
2020
pubmed:
18
9
2020
medline:
5
1
2021
entrez:
17
9
2020
Statut:
epublish
Résumé
Reovirus attachment protein σ1 is a trimeric molecule containing tail, body, and head domains. During infection, σ1 engages sialylated glycans and junctional adhesion molecule-A (JAM-A), triggering uptake into the endocytic compartment, where virions are proteolytically converted to infectious subvirion particles (ISVPs). Further disassembly allows σ1 release and escape of transcriptionally active reovirus cores into the cytosol. Electron microscopy has revealed a distinct conformational change in σ1 from a compact form on virions to an extended form on ISVPs. To determine the importance of σ1 conformational mobility, we used reverse genetics to introduce cysteine mutations that can cross-link σ1 by establishing disulfide bonds between structurally adjacent sites in the tail, body, and head domains. We detected phenotypic differences among the engineered viruses. A mutant with a cysteine pair in the head domain replicates with enhanced kinetics, forms large plaques, and displays increased avidity for JAM-A relative to the parental virus, mimicking properties of ISVPs. However, unlike ISVPs, particles containing cysteine mutations that cross-link the head domain uncoat and transcribe viral positive-sense RNA with kinetics similar to the parental virus and are sensitive to ammonium chloride, which blocks virion-to-ISVP conversion. Together, these data suggest that σ1 conformational flexibility modulates the efficiency of reovirus host cell attachment.
Identifiants
pubmed: 32938765
pii: JVI.01163-20
doi: 10.1128/JVI.01163-20
pmc: PMC7654274
pii:
doi:
Substances chimiques
Capsid Proteins
0
Cell Adhesion Molecules
0
Receptors, Cell Surface
0
Viral Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIDDK NIH HHS
ID : P30 DK058404
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI118887
Pays : United States
Informations de copyright
Copyright © 2020 American Society for Microbiology.
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