Glycan-mediated enhancement of reovirus receptor binding.
Animals
CHO Cells
Cell Adhesion Molecules
Cell Line
Cricetulus
Host-Pathogen Interactions
Models, Molecular
Polysaccharides
/ metabolism
Protein Binding
/ drug effects
Receptors, Cell Surface
/ drug effects
Receptors, Virus
/ drug effects
Reoviridae
/ drug effects
Viral Proteins
/ chemistry
Virus Attachment
/ drug effects
Virus Internalization
/ drug effects
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
01 10 2019
01 10 2019
Historique:
received:
26
02
2019
accepted:
06
09
2019
entrez:
3
10
2019
pubmed:
3
10
2019
medline:
7
1
2020
Statut:
epublish
Résumé
Viral infection is an intricate process that requires the concerted action of both viral and host cell components. Entry of viruses into cells is initiated by interactions between viral proteins and their cell surface receptors. Despite recent progress, the molecular mechanisms underlying the multistep reovirus entry process are poorly understood. Using atomic force microscopy, we investigated how the reovirus σ1 attachment protein binds to both α-linked sialic acid (α-SA) and JAM-A cell-surface receptors. We discovered that initial σ1 binding to α-SA favors a strong multivalent anchorage to JAM-A. The enhanced JAM-A binding by virions following α-SA engagement is comparable to JAM-A binding by infectious subvirion particles (ISVPs) in the absence of α-SA. Since ISVPs have an extended σ1 conformer, this finding suggests that α-SA binding triggers a conformational change in σ1. These results provide new insights into the function of viral attachment proteins in the initiation of infection and open new avenues for the use of reoviruses as oncolytic agents.
Identifiants
pubmed: 31575869
doi: 10.1038/s41467-019-12411-2
pii: 10.1038/s41467-019-12411-2
pmc: PMC6773860
doi:
Substances chimiques
Cell Adhesion Molecules
0
F11r protein, mouse
0
Polysaccharides
0
Receptors, Cell Surface
0
Receptors, Virus
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
Pagination
4460Subventions
Organisme : NIAID NIH HHS
ID : R01 AI038296
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI118887
Pays : United States
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