ArticleThe Journal of biological chemistry2008
Surface exposure of the HIV-1 env cytoplasmic tail LLP2 domain during the membrane fusion process: interaction with gp41 fusion core.
Article in The Journal of biological chemistry, 2008. 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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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.
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Who cites it
29 citing papers in PubMed, 42 citations in OpenAlex.
- Article
- A Conserved Tryptophan in the Envelope Cytoplasmic Tail Regulates HIV-1 Assembly and Spread.Viruses · 2022Article
- New Consensus pattern in Spike CoV-2: potential implications in coagulation process and cell-cell fusion.Cell death discovery · 2020Review
- Development of Protein- and Peptide-Based HIV Entry Inhibitors Targeting gp120 or gp41.Viruses · 2019Review
- Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein.Structure (London, England : 1993) · 2017Article
- Receptor binding domain based HIV vaccines.BioMed research international · 2015Review
- Enhanced central nervous system transduction with lentiviral vectors pseudotyped with RVG/HIV-1gp41 chimeric envelope glycoproteins.Journal of virology · 2014Article
- Structural and functional comparisons of retroviral envelope protein C-terminal domains: still much to learn.Viruses · 2014Review
- The frantic play of the concealed HIV envelope cytoplasmic tail.Retrovirology · 2013Review
- Molecular identification, cloning and characterization of transmitted/founder HIV-1 subtype A, D and A/D infectious molecular clones.Virology · 2013Article
- C-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic.The Journal of general virology · 2013Review
- The tale of the long tail: the cytoplasmic domain of HIV-1 gp41.Journal of virology · 2013Review
- Article
- Identification of a human protein-derived HIV-1 fusion inhibitor targeting the gp41 fusion core structure.PloS one · 2013Article
- Study of the HIV-2 Env cytoplasmic tail variability and its impact on Tat, Rev and Nef.PloS one · 2013Article
- A bivalent recombinant protein inactivates HIV-1 by targeting the gp41 prehairpin fusion intermediate induced by CD4 D1D2 domains.Retrovirology · 2012Article
- Evidence against extracellular exposure of a highly immunogenic region in the C-terminal domain of the simian immunodeficiency virus gp41 transmembrane protein.Journal of virology · 2012Article
- Targeting HIV-1 gp41-induced fusion and pathogenesis for anti-viral therapy.Current topics in medicinal chemistry · 2011Review
- Highly conserved structural properties of the C-terminal tail of HIV-1 gp41 protein despite substantial sequence variation among diverse clades: implications for functions in viral replication.The Journal of biological chemistry · 2011Article
- HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation.Journal of molecular biology · 2011Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
HIV-1 gp41 cytoplasmic tail (CT) is highly conserved among HIV-1 isolates, particularly the region designated lentivirus lytic peptide (LLP1-2), which includes two alpha-helical domains LLP1 and LLP2. Although the gp41 CT is recognized as a modulator of viral fusogenicity, little is known about the regulatory mechanism of this region in the viral fusion process. Here we report that anti-LLP1-2 and anti-LLP2 antibodies (IgG) inhibited HIV-1 Env-mediated cell fusion and bound to the interface between effector and target cells at a suboptimal temperature (31.5 degrees C), which slows down the fusion process and prolongs the fusion intermediate state. This suggests that LLP1-2, especially the LLP2 region located inside the viral membrane, is transiently exposed on the membrane surface during the fusion process. Synthetic LLP2 peptide could bind to the gp41 six-helix bundle core with high binding affinity. These results suggest that the gp41 CT may interact with the gp41 core, via the surface-exposed LLP2 domain, to regulate Env-mediated membrane fusion.
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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.