ArticleJournal of virology2008
Cysteines flanking the internal fusion peptide are required for the avian sarcoma/leukosis virus glycoprotein to mediate the lipid mixing stage of fusion with high efficiency.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells.Virology · 2018Review
- Visualization of the two-step fusion process of the retrovirus avian sarcoma/leukosis virus by cryo-electron tomography.Journal of virology · 2012Article
- Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change.Journal of virology · 2012Article
- Retrovirus entry by endocytosis and cathepsin proteases.Advances in virology · 2012Article
- Binding of more than one Tva800 molecule is required for ASLV-A entry.Retrovirology · 2011Article
- Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- An antibody directed against the fusion peptide of Junin virus envelope glycoprotein GPC inhibits pH-induced membrane fusion.Journal of virology · 2010Article
- Studies of the "chain reversal regions" of the avian sarcoma/leukosis virus (ASLV) and ebolavirus fusion proteins: analogous residues are important, and a His residue unique to EnvA affects the pH dependence of ASLV entry.Journal of virology · 2010Article
- SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion.Virology · 2009Article
- A charged second-site mutation in the fusion peptide rescues replication of a mutant avian sarcoma and leukosis virus lacking critical cysteine residues flanking the internal fusion domain.Journal of virology · 2009Article
- Article
- Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
We previously showed that the cysteines flanking the internal fusion peptide of the avian sarcoma/leukosis virus subtype A (ASLV-A) Env (EnvA) are important for infectivity and cell-cell fusion. Here we define the stage of fusion at which the cysteines are required. The flanking cysteines are dispensable for receptor-triggered membrane association but are required for the lipid mixing step of fusion, which, interestingly, displays a high pH onset and a biphasic profile. Second-site mutations that partially restore infection partially restore lipid mixing. These findings indicate that the cysteines flanking the internal fusion peptide of EnvA (and perhaps by analogy Ebola virus glycoprotein) are important for the foldback stage of the conformational changes that lead to membrane merger.
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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.