ArticleThe Journal of biological chemistry2019
Fully hydrophobic HIV gp41 adopts a hemifusion-like conformation in phospholipid bilayers.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Lipid Acyl Chain-Driven α-Synuclein Fibril Polymorphisms and Neuronal Pathologies.ACS chemical neuroscience · 2026Article
- Pseudo-Phosphorylated Tau Forms Paired Helical Filaments in the Presence of High-Curvature Cholesterol-Containing Lipid Membranes.Journal of the American Chemical Society · 2025Article
- How Cell-Penetrating Peptides Behave Differently from Pore-Forming Peptides: Structure and Stability of Induced Transmembrane Pores.Journal of the American Chemical Society · 2023Article
- Article
- Interactions of HIV gp41's membrane-proximal external region and transmembrane domain with phospholipid membranes fromBiochimica et biophysica acta. Biomembranes · 2021Article
- Virus Structures and Dynamics by Magic-Angle Spinning NMR.Annual review of virology · 2021Review
- Mechanistic insights of host cell fusion of SARS-CoV-1 and SARS-CoV-2 from atomic resolution structure and membrane dynamics.Biophysical chemistry · 2020Review
- Review
- Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations.Journal of molecular biology · 2020Article
- Viral Membrane Fusion and the Transmembrane Domain.Viruses · 2020Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The HIV envelope glycoprotein mediates virus entry into target cells by fusing the virus lipid envelope with the cell membrane. This process requires large-scale conformational changes of the fusion protein gp41. Current understanding of the mechanisms with which gp41 induces membrane merger is limited by the fact that the hydrophobic N-terminal fusion peptide (FP) and C-terminal transmembrane domain (TMD) of the protein are challenging to characterize structurally in the lipid bilayer. Here we have expressed a gp41 construct that contains both termini, including the FP, the fusion peptide-proximal region (FPPR), the membrane-proximal external region (MPER), and the TMD. These hydrophobic domains are linked together by a shortened water-soluble ectodomain. We reconstituted this "short NC" gp41 into a virus-mimetic lipid membrane and conducted solid-state NMR experiments to probe the membrane-bound conformation and topology of the protein.
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Registered trials
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