ArticleJournal of virology1994
The membrane-associated and secreted forms of the respiratory syncytial virus attachment glycoprotein G are synthesized from alternative initiation codons.
Article in Journal of virology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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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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Who cites it
70 citing papers in PubMed, 159 citations in OpenAlex.
- Review
- The soluble G protein of respiratory syncytial virus promotes viral dissemination via TLR2-mediated NLRP3 priming and pyroptosis.Npj viruses · 2026Article
- Rational design 2.0: transitioning from static structural biology to computational prioritization and iterative vaccine optimization for RSV.Frontiers in immunology · 2026Review
- RSV Vaccines: Targeting Prefusion F and G Proteins from Structural Design to Clinical Application.Vaccines · 2025Review
- Recent advances in the prevention and treatment of respiratory syncytial virus disease.The Journal of general virology · 2025Review
- Secretory Expression and Purification of Respiratory Syncytial Virus G and F Ectodomain in Human Cells.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Introduction to Respiratory Syncytial Virus.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Respiratory syncytial virus glycoprotein G impedes CXNpj viruses · 2024Article
- Approaches to the Prevention and Treatment of Respiratory Syncytial Virus Infection in Children: Rationale and Progress to Date.Paediatric drugs · 2024Article
- New Insights on Respiratory Syncytial Virus Prevention.Vaccines · 2023Review
- Review and Update of Active and Passive Immunization Against Respiratory Syncytial Virus.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023Review
- Structure-Based Design and Antigenic Validation of Respiratory Syncytial Virus G Immunogens.Journal of virology · 2022Article
- Review
- Activation of TLR4 by viral glycoproteins: A double-edged sword?Frontiers in microbiology · 2022Review
- Article
- Immunogenicity and inflammatory properties of respiratory syncytial virus attachment G protein in cotton rats.PloS one · 2021Article
- Respiratory syncytial virus: from pathogenesis to potential therapeutic strategies.International journal of biological sciences · 2021Review
- Revisiting respiratory syncytial virus's interaction with host immunity, towards novel therapeutics.Cellular and molecular life sciences : CMLS · 2020Review
- Understudied Factors Influencing Fc-Mediated Immune Responses against Viral Infections.Vaccines · 2019Review
- A Contemporary View of Respiratory Syncytial Virus (RSV) Biology and Strain-Specific Differences.Pathogens (Basel, Switzerland) · 2019Review
10 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Respiratory syncytial (RS) virus synthesizes two mature forms of its attachment glycoprotein G: an anchored type II integral membrane form and a smaller form that is secreted into the medium. Here we demonstrate that these two forms are synthesized as distinct primary translation products of a single species of G protein mRNA by initiation at either of two different AUGs. Mutant cDNAs which eliminated one of the other of the two AUG codons near the 5' end of the G gene open reading frame were constructed. Analysis of the proteins synthesized from these cDNAs, either by translation of transcripts in a cell-free system or in cells infected with recombinant vaccinia viruses containing either one of the mutant cDNAs, showed that elimination of either the first or the second of these AUG codons abrogated the synthesis of the membrane-anchored or the secreted form of the protein, respectively. Additionally, two unglycosylated forms of G protein which comigrated with the unglycosylated G proteins expressed by these recombinant viruses were detected in RS virus-infected cells. Since the second AUG encodes a methionine residue that lies near the middle of the signal/anchor domain, initiation at this codon resulted in a protein with a hydrophobic amino terminus. This form of the glycoprotein was efficiently secreted from cells infected with the vaccinia virus recombinant, and the amino-terminal sequence of this protein was identical to that of G protein secreted from RS virus-infected cells. Our results demonstrate that the secreted form of RS virus G protein is produced by initiation at the second AUG codon of the G open reading frame, followed by proteolytic removal of the signal/anchor domain.
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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.