ArticleBiochemistry2012
HIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 57 citations in OpenAlex.
- Article
- Lessons Learnt from COVID-19: Computational Strategies for Facing Present and Future Pandemics.International journal of molecular sciences · 2023Review
- SARS-CoV-2-host cell surface interactions and potential antiviral therapies.Interface focus · 2022Review
- Membranotropic and biological activities of the membrane fusion peptides from SARS-CoV spike glycoprotein: The importance of the complete internal fusion peptide domain.Biochimica et biophysica acta. Biomembranes · 2021Article
- Molecular biology of the SARs-CoV-2 spike protein: A review of current knowledge.Journal of medical virology · 2021Review
- Peptide Triazole Thiol Irreversibly Inactivates Metastable HIV-1 Env by Accessing Conformational Triggers Intrinsic to Virus-Cell Entry.Microorganisms · 2021Article
- Article
- Immunogenicity of HIV-1-Based Virus-Like Particles with Increased Incorporation and Stability of Membrane-Bound Env.Vaccines · 2021Article
- Mechanistic insights of host cell fusion of SARS-CoV-1 and SARS-CoV-2 from atomic resolution structure and membrane dynamics.Biophysical chemistry · 2020Review
- Viral Membrane Fusion and the Transmembrane Domain.Viruses · 2020Review
- Fully hydrophobic HIV gp41 adopts a hemifusion-like conformation in phospholipid bilayers.The Journal of biological chemistry · 2019Article
- A Hydrophobic Target: Using the Paramyxovirus Fusion Protein Transmembrane Domain To Modulate Fusion Protein Stability.Journal of virology · 2019Article
- Oligomeric Structure and Three-Dimensional Fold of the HIV gp41 Membrane-Proximal External Region and Transmembrane Domain in Phospholipid Bilayers.Journal of the American Chemical Society · 2018Article
- Stability and Water Accessibility of the Trimeric Membrane Anchors of the HIV-1 Envelope Spikes.Journal of the American Chemical Society · 2017Article
- Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Hendra virus fusion protein transmembrane domain contributes to pre-fusion protein stability.The Journal of biological chemistry · 2017Article
- Identification of the Fusion Peptide-Containing Region in Betacoronavirus Spike Glycoproteins.Journal of virology · 2016Article
- Fusion of Enveloped Viruses in Endosomes.Traffic (Copenhagen, Denmark) · 2016Review
- Article
- The Interaction between Influenza HA Fusion Peptide and Transmembrane Domain Affects Membrane Structure.Biophysical journal · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Fusion of the human immunodeficiency virus (HIV) with target cells is mediated by the gp41 subunit of the envelope protein. Mutation and deletion studies within the transmembrane domain (TMD) of intact gp41 influenced its fusion activity. In addition, current models suggest that the TMD is in proximity with the fusion peptide (FP) at the late fusion stages, but there are no direct experimental data to support this hypothesis. Here, we investigated the TMD focusing on two regions: the N-terminal containing the GxxxG motif and the C-terminal containing the GLRI motif, which is conserved among the TMDs of HIV and the T-cell receptor. Studies utilizing the ToxR expression system combined with synthetic peptides and their fluorescent analogues derived from TMD revealed that the GxxxG motif is important for TMD self-association, whereas the C-terminal region is for its heteroassociation with FP. Functionally, all three TMD peptides induced lipid mixing that was enhanced significantly upon mixing with FP. Furthermore, the TMD peptides inhibited virus-cell fusion apparently through their interaction with their endogenous counterparts. Notably, the R2E mutant (in the GLRI) was significantly less potent than the two others. Overall, our findings provide experimental evidence that HIV-1 TMD contributes to membrane assembly and function of the HIV-1 envelope. Owing to similarities between functional domains within viruses, these findings suggest that the TMDs and FPs may contribute similarly in other viruses as well.
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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.