ArticleJournal of virology2007
Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains.
Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
42 citing papers in PubMed, 57 citations in OpenAlex.
- The Lassa Virus Stable Signal Peptide Undergoes a Conformational Change to Aid Viral Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Lassa virus protein-protein interactions as mediators of Lassa fever pathogenesis.Virology journal · 2025Review
- Architectural organization andJournal of virology · 2024Article
- Structural and molecular biology of Sabiá virus.Experimental biology and medicine (Maywood, N.J.) · 2023Review
- Article
- Lassa virus glycoprotein complex review: insights into its unique fusion machinery.Bioscience reports · 2022Review
- Activation of the PDGF β Receptor by a Persistent Artificial Signal Peptide.Journal of molecular biology · 2021Article
- The late endosome-resident lipid bis(monoacylglycero)phosphate is a cofactor for Lassa virus fusion.PLoS pathogens · 2021Article
- Second-Generation Live-Attenuated Candid#1 Vaccine Virus Resists Reversion and Protects against Lethal Junín Virus Infection in Guinea Pigs.Journal of virology · 2021Article
- Characterizing the Lassa Virus Envelope Glycoprotein Membrane Proximal External Region for Its Role in Fusogenicity.Virologica Sinica · 2021Article
- Recent Advances in Bunyavirus Glycoprotein Research: Precursor Processing, Receptor Binding and Structure.Viruses · 2021Review
- Identification of the dietary supplement capsaicin as an inhibitor of Lassa virus entry.Acta pharmaceutica Sinica. B · 2020Article
- Biological Characterization of Conserved Residues within the Cytoplasmic Tail of the Pichinde Arenaviral Glycoprotein Subunit 2 (GP2).Journal of virology · 2019Article
- Screening and Identification of Lassa Virus Entry Inhibitors from an FDA-Approved Drug Library.Journal of virology · 2018Article
- Lassa virus glycoprotein: stopping a moving target.Current opinion in virology · 2018Review
- Structural basis for antibody-mediated neutralization of Lassa virus.Science (New York, N.Y.) · 2017Article
- Transcription and replication mechanisms of Bunyaviridae and Arenaviridae L proteins.Virus research · 2017Review
- Characterization of the Glycoprotein Stable Signal Peptide in Mediating Pichinde Virus Replication and Virulence.Journal of virology · 2016Article
- Structure-function relationship of the mammarenavirus envelope glycoprotein.Virologica Sinica · 2016Review
- Myristoylation of the Arenavirus Envelope Glycoprotein Stable Signal Peptide Is Critical for Membrane Fusion but Dispensable for Virion Morphogenesis.Journal of virology · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The stable signal peptide (SSP) of the lymphocytic choriomeningitis virus surface glycoprotein precursor has several unique characteristics. The SSP is unusually long, at 58 amino acids, and contains two hydrophobic domains, and its sequence is highly conserved among both Old and New World arenaviruses. To better understand the functions of the SSP, a panel of point and deletion mutants was created by in vitro mutagenesis to target the highly conserved elements within the SSP. We were also able to confirm critical residues required for separate SSP functions by trans-complementation. Using these approaches, it was possible to resolve functional domains of the SSP. In characterizing our SSP mutants, we discovered that the SSP is involved in several distinct functions within the viral life cycle, beyond translocation of the viral surface glycoprotein precursor into the endoplasmic reticulum lumen. The SSP is required for efficient glycoprotein expression, posttranslational maturation cleavage of GP1 and GP2 by SKI-1/S1P protease, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.