New World arenavirus clade C, but not clade A and B viruses, utilizes alpha-dystroglycan as its major receptor.

Détails

ID Serval
serval:BIB_DFE95CFFD65D
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
New World arenavirus clade C, but not clade A and B viruses, utilizes alpha-dystroglycan as its major receptor.
Périodique
Journal of Virology
Auteur⸱e⸱s
Spiropoulou C.F., Kunz S., Rollin P.E., Campbell K.P., Oldstone M.B.
ISSN
0022-538X (Print)
ISSN-L
0022-538X
Statut éditorial
Publié
Date de publication
2002
Volume
76
Numéro
10
Pages
5140-5146
Langue
anglais
Résumé
Alpha-dystroglycan (alpha-DG) has been identified as a major receptor for lymphocytic choriomeningitis virus (LCMV) and Lassa virus, two Old World arenaviruses. The situation with New World arenaviruses is less clear: previous studies demonstrated that Oliveros virus also exhibited high-affinity binding to alpha-DG but that Guanarito virus did not. To extend these initial studies, several additional Old and New World arenaviruses were screened for entry into mouse embryonic stem cells possessing or lacking alpha-DG. In addition, representative viruses were further analyzed for direct binding to alpha-DG by means of a virus overlay protein blot assay technique. These studies indicate that Old World arenaviruses use alpha-DG as a major receptor, whereas, of the New World arenaviruses, only clade C viruses (i.e., Oliveros and Latino viruses) use alpha-DG as a major receptor. New World clade A and B arenaviruses, which include the highly pathogenic Machupo, Guanarito, Junin, and Sabia viruses, appear to use a different receptor or coreceptor for binding. Previous studies with LCMV have suggested the need for a small aliphatic amino acid at LCMV GP1 glycoprotein amino acid position 260 to allow high-affinity binding to alpha-DG. As reported herein, this requirement appears to be broadly applicable to the arenaviruses as determined by more extensive analysis of alpha-DG receptor usage and GP1 sequences of Old and New World arenaviruses. In addition, GP1 amino acid position 259 also appears to be important, since all arenaviruses showing high-affinity alpha-DG binding possess a bulky aromatic amino acid (tyrosine or phenylalanine) at this position.
Mots-clé
Amino Acid Sequence, Animals, Arenaviruses, New World/classification, Arenaviruses, New World/genetics, Arenaviruses, Old World/classification, Arenaviruses, Old World/physiology, Cell Line, Cytoskeletal Proteins/metabolism, Cytoskeletal Proteins/physiology, Dystroglycans, Dystrophin/metabolism, Dystrophin/physiology, Glycoproteins/genetics, Membrane Glycoproteins/metabolism, Membrane Glycoproteins/physiology, Mice, Molecular Sequence Data, Phylogeny, Receptors, Virus/metabolism, Sequence Alignment, Stem Cells/metabolism, Stem Cells/virology, Viral Envelope Proteins/genetics, Virus Replication
Pubmed
Web of science
Open Access
Oui
Création de la notice
17/04/2013 11:56
Dernière modification de la notice
20/08/2019 16:04
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