ArticleVirology2013
The role of proteolytic processing and the stable signal peptide in expression of the Old World arenavirus envelope glycoprotein ectodomain.
Article in Virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Development of a Conditional Replication System Using a Lassa Virus Glycoprotein Complex-Encoding Retroviral Vector for Isolating Resistant Variants to Inhibitors in BSL-2.International journal of molecular sciences · 2026Article
- Architectural organization andJournal of virology · 2024Article
- Lymphocytic choriomeningitis arenavirus requires cellular COPI and AP-4 complexes for efficient virion production.Journal of virology · 2024Article
- Article
- Structural basis for antibody-mediated neutralization of lymphocytic choriomeningitis virus.Cell chemical biology · 2023Article
- Design, Synthesis, and Biological Evaluation of Benzimidazole Derivatives as Potential Lassa Virus Inhibitors.Molecules (Basel, Switzerland) · 2023Article
- CD164 is a host factor for lymphocytic choriomeningitis virus entry.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Lassa virus glycoprotein complex review: insights into its unique fusion machinery.Bioscience reports · 2022Review
- Article
- Identification of a clinical compound losmapimod that blocks Lassa virus entry.Antiviral research · 2019Article
- Hemorrhagic Fever-Causing Arenaviruses: Lethal Pathogens and Potent Immune Suppressors.Frontiers in immunology · 2019Review
- Screening and Identification of Lassa Virus Entry Inhibitors from an FDA-Approved Drug Library.Journal of virology · 2018Article
- Arenavirus stable signal peptide is the keystone subunit for glycoprotein complex organization.mBio · 2014Article
- Evolution of recombinant lymphocytic choriomeningitis virus/Lassa virus in vivo highlights the importance of the GPC cytosolic tail in viral fitness.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
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.
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