ArticleJournal of virology1994
Characterization of the putative fusogenic domain in vesicular stomatitis virus glycoprotein G.
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 44 papers.
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Who cites it
44 citing papers in PubMed, 96 citations in OpenAlex.
- Exploring the influence of anionic lipids in the host cell membrane on viral fusion.Biochemical Society transactions · 2024Review
- The interaction of viral fusion peptides with lipid membranes.Biophysical journal · 2022Article
- Monomeric Intermediates Formed by Vesiculovirus Glycoprotein during Its Low-pH-induced Structural Transition.Journal of molecular biology · 2018Review
- Dendritic cell-targeted lentiviral vector immunization uses pseudotransduction and DNA-mediated STING and cGAS activation.Science immunology · 2017Article
- Structural intermediates in the fusion-associated transition of vesiculovirus glycoprotein.The EMBO journal · 2017Article
- Entry of rhabdoviruses into animal cells.Advances in experimental medicine and biology · 2013Review
- Internalization and fusion mechanism of vesicular stomatitis virus and related rhabdoviruses.Future virology · 2010Article
- Mutagenesis of the fusion peptide-like domain of hepatitis C virus E1 glycoprotein: involvement in cell fusion and virus entry.Journal of biomedical science · 2009Article
- Class III viral membrane fusion proteins.Current opinion in structural biology · 2009Review
- Enzootic nasal tumor virus envelope requires a very acidic pH for fusion activation and infection.Journal of virology · 2008Article
- Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity.Journal of virology · 2007Article
- Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein B.Journal of virology · 2007Article
- Fusion of microglia with pyramidal neurons after retroviral infection.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Probing the interaction between vesicular stomatitis virus and phosphatidylserine.European biophysics journal : EBJ · 2006Article
- Biological differences between vesicular stomatitis virus Indiana and New Jersey serotype glycoproteins: identification of amino acid residues modulating pH-dependent infectivity.Journal of virology · 2005Article
- The ectodomain of herpes simplex virus glycoprotein H contains a membrane alpha-helix with attributes of an internal fusion peptide, positionally conserved in the herpesviridae family.Journal of virology · 2005Article
- Conformation- and fusion-defective mutations in the hypothetical phospholipid-binding and fusion peptides of viral hemorrhagic septicemia salmonid rhabdovirus protein G.Journal of virology · 2004Article
- The hypervariable region 1 of the E2 glycoprotein of hepatitis C virus binds to glycosaminoglycans, but this binding does not lead to infection in a pseudotype system.Journal of virology · 2004Article
- The membrane-proximal region of vesicular stomatitis virus glycoprotein G ectodomain is critical for fusion and virus infectivity.Journal of virology · 2003Article
- Vesicular stomatitis virus glycoprotein is a determinant of pathogenesis in swine, a natural host.Journal of virology · 2003Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The envelope glycoprotein G of vesicular stomatitis virus induces membrane fusion at low pH. Site-directed mutagenesis of specific amino acids within a segment spanning amino acids 123 to 137 of G protein, which is highly conserved in vesiculoviruses and was previously shown by us to be involved in fusogenic activity (Y. Li, C. Drone, E. Sat, and H. P. Ghosh, J. Virol. 67:4070-4077, 1993), was used to determine the role of this region in low-pH-induced membrane fusion. The mutant glycoproteins expressed in COS cells were assayed for acid-pH-induced cell-cell fusion. Substitution of the variant Pro-123 with Leu had no effect on the fusogenic activity, while substitution of conserved Phe-125 and Asp-137 with Tyr and Asn, respectively, shifted the pH optimum of membrane fusion to a more acidic pH value and decreased the fusion efficiency. The deletion of amino acid residues 124 to 127, 131 to 137, or 124 to 137 produced mutants defective in transport. Mutation of the conserved residues Gly-124 and Pro-127 to Ala and to Gly or Leu, respectively, inhibited cell-cell fusion activity by about 90% without affecting transport of the mutant proteins to the cell surface, suggesting that these two residues may be present within the fusion peptide and thus may be directly involved in fusion. This highly conserved domain containing neutral amino acids of G protein may therefore represent the putative fusion domain of vesicular stomatitis virus G protein.
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