ArticleJournal of virology2007
Signal peptide requirements for lymphocytic choriomeningitis virus glycoprotein C maturation and virus infectivity.
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 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed.
- Mammarenaviruses depend on endogenous fatty acid synthesis in cell culture systems.Journal of lipid research · 2026Article
- 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
- Recent Advances in Bunyavirus Glycoprotein Research: Precursor Processing, Receptor Binding and Structure.Viruses · 2021Review
- 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
- Structure-function relationship of the mammarenavirus envelope glycoprotein.Virologica Sinica · 2016Review
- Bunyamwera orthobunyavirus glycoprotein precursor is processed by cellular signal peptidase and signal peptide peptidase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV.Nature structural & molecular biology · 2016Article
- Acidic pH-Induced Conformations and LAMP1 Binding of the Lassa Virus Glycoprotein Spike.PLoS pathogens · 2016Article
- Membrane proteins of arterivirus particles: structure, topology, processing and function.Virus research · 2014Review
- Arenavirus stable signal peptide is the keystone subunit for glycoprotein complex organization.mBio · 2014Article
- Cell surface-associated anti-MUC1-derived signal peptide antibodies: implications for cancer diagnostics and therapy.PloS one · 2014Article
- Genomic analysis and pathogenic characteristics of lymphocytic choriomeningitis virus strains isolated in Japan.Comparative medicine · 2012Article
- The myristate moiety and amino terminus of vaccinia virus l1 constitute a bipartite functional region needed for entry.Journal of virology · 2012Article
- Review
- Complete genome sequences of avian paramyxovirus serotype 6 prototype strain Hong Kong and a recent novel strain from Italy: evidence for the existence of subgroups within the serotype.Virus research · 2010Article
- Characterization of Lassa virus glycoprotein oligomerization and influence of cholesterol on virus replication.Journal of virology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insertion of the lymphocytic choriomeningitis virus (LCMV) precursor glycoprotein C (GP-C) into the membrane of the endoplasmic reticulum is mediated by an unusual signal peptide (SP(GP-C)). It is comprised of 58 amino acid residues and contains an extended hydrophilic N-terminal region, two hydrophobic regions, and a short C-terminal region. After cleavage by signal peptidase, SP(GP-C) accumulates in cells and virus particles. In the present study, we identified the LCMV SP(GP-C) as being an essential component of the GP complex and show that the different regions of SP(GP-C) are required for distinct steps in GP maturation and virus infectivity. More specifically, we show that one hydrophobic region of SP(GP-C) is sufficient for the membrane insertion of GP-C, while both hydrophobic regions are required for the processing and cell surface expression of the GPs. The N-terminal region of SP(GP-C), on the other hand, is essential for pseudoviral infection of target cells. Furthermore, we show that unmyristoylated SP(GP-C) exposes its N-terminal region to the exoplasmic side. This SP(GP-C) can promote GP-C maturation but is defective in pseudoviral infection. Myristoylation and topology of SP(GP-C) in the membrane may thus hold the key to an understanding of the role of SP(GP-C) in GP-C complex maturation and LCMV infectivity.
Indexed as
Identifiers
What OpenQuestion holds
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.