The role of proteolytic processing and the stable signal peptide in expression of the Old World arenavirus envelope glycoprotein ectodomain.

Détails

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Etat: Serval
Version: de l'auteur
ID Serval
serval:BIB_7DE57711738A
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The role of proteolytic processing and the stable signal peptide in expression of the Old World arenavirus envelope glycoprotein ectodomain.
Périodique
Virology
Auteur(s)
Burri D.J., Pasquato A., Ramos da Palma J., Igonet S., Oldstone M.B., Kunz S.
ISSN
1096-0341 (Electronic)
ISSN-L
0042-6822
Statut éditorial
Publié
Date de publication
2013
Volume
436
Numéro
1
Pages
127-133
Langue
anglais
Notes
Publication types: Journal ArticlePublication Status: ppublish
Résumé
Maturation of the arenavirus GP precursor (GPC) involves proteolytic processing by cellular signal peptidase and the proprotein convertase subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P), yielding a tripartite complex comprised of a stable signal peptide (SSP), the receptor-binding GP1, and the fusion-active transmembrane GP2. Here we investigated the roles of SKI-1/S1P processing and SSP in the biosynthesis of the recombinant GP ectodomains of lymphocytic choriomeningitis virus (LCMV) and Lassa virus (LASV). When expressed in mammalian cells, the LCMV and LASV GP ectodomains underwent processing by SKI-1/S1P, followed by dissociation of GP1 from GP2. The GP2 ectodomain spontaneously formed trimers as revealed by chemical cross-linking. The endogenous SSP, known to be crucial for maturation and transport of full-length arenavirus GPC was dispensable for processing and secretion of the soluble GP ectodomain, suggesting a specific role of SSP in the stable prefusion conformation and transport of full-length GPC.
Pubmed
Web of science
Open Access
Oui
Création de la notice
21/02/2013 18:41
Dernière modification de la notice
08/05/2019 20:58
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