ArticleJournal of virology2000
An evolutionarily conserved positively charged amino acid in the putative membrane-spanning domain of the foamy virus envelope protein controls fusion activity.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 51 citations in OpenAlex.
- Plasma antibodies from humans infected with zoonotic simian foamy virus do not inhibit cell-to-cell transmission of the virus despite binding to the surface of infected cells.PLoS pathogens · 2022Observational
- Review
- Structure of the transmembrane domain of HIV-1 envelope glycoprotein.The FEBS journal · 2017Review
- Cryo-electron Microscopy Structure of the Native Prototype Foamy Virus Glycoprotein and Virus Architecture.PLoS pathogens · 2016Article
- Cocirculation of Two env Molecular Variants, of Possible Recombinant Origin, in Gorilla and Chimpanzee Simian Foamy Virus Strains from Central Africa.Journal of virology · 2015Article
- An N-terminal domain helical motif of Prototype Foamy Virus Gag with dual functions essential for particle egress and viral infectivity.Retrovirology · 2013Article
- Foamy virus budding and release.Viruses · 2013Review
- Review
- Genetic characterization of simian foamy viruses infecting humans.Journal of virology · 2012Article
- Differential pH-dependent cellular uptake pathways among foamy viruses elucidated using dual-colored fluorescent particles.Retrovirology · 2012Article
- Conserved arginine residue in the membrane-spanning domain of HIV-1 gp41 is required for efficient membrane fusion.Protein & cell · 2011Article
- Molecular biology of foamy viruses.Medical microbiology and immunology · 2010Review
- The Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: analysis of transmembrane domain length and sequence requirements.Journal of virology · 2009Article
- Subviral particle release determinants of prototype foamy virus.Journal of virology · 2008Article
- Characterization of the prototype foamy virus envelope glycoprotein receptor-binding domain.Journal of virology · 2006Article
- Ubiquitination of the prototype foamy virus envelope glycoprotein leader peptide regulates subviral particle release.Journal of virology · 2005Article
- N-terminal Gag domain required for foamy virus particle assembly and export.Journal of virology · 2005Article
- Analysis and function of prototype foamy virus envelope N glycosylation.Journal of virology · 2005Article
- Characterization of prototype foamy virus gag late assembly domain motifs and their role in particle egress and infectivity.Journal of virology · 2005Article
- The many mechanisms of viral membrane fusion proteins.Current topics in microbiology and immunology · 2005Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Foamy viruses (FVs) are highly fusogenic, and their replication induces massive syncytium formation in infected cell cultures which is believed to be mediated by expression of the envelope (Env) protein. The FV Env is essential for virus particle egress. The unusually long putative membrane-spanning domain (MSD) of the transmembrane subunit carries dispersed charged amino acids and has an important function for particle envelopment. To better understand the capsid-envelope interaction and Env-mediated cell fusion, we generated a variety of FV MSD mutations. C-terminal deletions revealed the cytoplasmic domain to be dispensable but the full-length MSD to be required for fusogenic activity. The N-terminal 15 amino acids of the MSD were found to be sufficient for membrane anchorage and promotion of FV particle release. Expression of wild-type Env protein rarely induced syncytia due to intracellular retention. Coexpression with FV Gag-Pol resulted in particle export and a dramatic increase in fusion activity. A nonconservative mutation of K(959) in the middle of the putative MSD resulted in increased fusogenic activity of Env in the absence of Gag-Pol due to enhanced cell surface expression as well as structural changes in the mutant proteins. Coexpression with Gag-Pol resulted in a further increase in the fusion activity of mutant FV Env proteins. Our results suggest that an interaction between the viral capsid and Env is required for FV-induced giant-cell formation and that the positive charge in the MSD is an important determinant controlling intracellular transport and fusogenic activity of the FV Env protein.
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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.