Alpha-dystroglycan can mediate arenavirus infection in the absence of beta-dystroglycan.

Détails

ID Serval
serval:BIB_F9C029549DFB
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Alpha-dystroglycan can mediate arenavirus infection in the absence of beta-dystroglycan.
Périodique
Virology
Auteur(s)
Kunz S., Campbell K.P., Oldstone M.B.
ISSN
0042-6822 (Print)
ISSN-L
0042-6822
Statut éditorial
Publié
Date de publication
2003
Volume
316
Numéro
2
Pages
213-220
Langue
anglais
Résumé
Dystroglycan (DG) is a highly versatile cell surface molecule that provides a molecular link between the extracellular matrix (ECM) and the actin-based cytoskeleton. Encoded by a single gene, DG is posttranslationally processed to form alpha-DG, a peripheral protein identified as the cellular receptor for lymphocytic choriomeningitis virus (LCMV) and Lassa fever virus (LFV), and the membrane-spanning subunit beta-DG. The link of beta-DG to the actin-based cytoskeleton and its association with the cellular signal transduction network suggest that it may function as an essential cofactor for the activity of alpha-DG as a virus receptor. To address this issue, we constructed a deletion mutant lacking the cytoplasmic domain of beta-DG and a C-terminal fusion between alpha-DG and the transmembrane domain of PDGF receptor. Both mutants were functional as virus receptors, indicating that beta-DG does not act as a cofactor with alpha-DG for arenavirus binding and entry. These observations are in agreement with the fact that LCMV infection is independent from the structural integrity of the actin-based cytoskeleton and suggest that alpha-DG functions primarily in the attachment of arenaviruses to the cell surface.
Mots-clé
Animals, Cricetinae, Cytoskeletal Proteins/physiology, Dystroglycans, Lymphocytic Choriomeningitis/etiology, Membrane Glycoproteins/physiology, Receptors, Virus/physiology
Pubmed
Web of science
Création de la notice
17/04/2013 12:56
Dernière modification de la notice
03/03/2018 22:54
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