ArticleProtein science : a publication of the Protein Society2010
Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 66 citations in OpenAlex.
- Advances in Viroporin Function and Structure: A Comparative Analysis of Alphavirus 6K with Well-Characterized Viroporins.Viruses · 2025Review
- Highly versatile small virus-encoded proteins in cellular membranes: A structural perspective on how proteins' inherent conformational plasticity couples with host membranes' properties to control cellular processes.Journal of structural biology: X · 2025Article
- Differences in Oligomerization of the SARS-CoV-2 Envelope Protein, Poliovirus VP4, and HIV Vpu.Biochemistry · 2024Article
- HIV-1 Vpu protein forms stable oligomers in aqueous solution via its transmembrane domain self-association.Scientific reports · 2023Article
- Rapid Determination of the Topology of Oligomeric α-Helical Membrane Proteins by Water- and Lipid-Edited Methyl NMR.The journal of physical chemistry. B · 2023Article
- Differences in Oligomerization of the SARS-CoV-2 Envelope Protein, Poliovirus VP4, and HIV Vpu.bioRxiv : the preprint server for biology · 2023Article
- HIV-1 Vpu protein forms stable oligomers in aqueous solution via its transmembrane domain self-association.bioRxiv : the preprint server for biology · 2023Article
- Insights into the oligomeric structure of the HIV-1 Vpu protein.Journal of structural biology · 2023Article
- SARS-CoV-2 Envelope Protein Forms Clustered Pentamers in Lipid Bilayers.Biochemistry · 2022Article
- Virus Structures and Dynamics by Magic-Angle Spinning NMR.Annual review of virology · 2021Review
- Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers.Nature structural & molecular biology · 2020Article
- Structure and Drug Binding of the SARS-CoV-2 Envelope Protein in Phospholipid Bilayers.Research square · 2020Article
- FRET Analysis of the Promiscuous yet Specific Interactions of the HIV-1 Vpu Transmembrane Domain.Biophysical journal · 2017Article
- Endocytic activity of HIV-1 Vpu: Phosphoserine-dependent interactions with clathrin adaptors.Traffic (Copenhagen, Denmark) · 2017Article
- Flexible Proteins at the Origin of Life.Life (Basel, Switzerland) · 2017Article
- Novel Acylguanidine-Based Inhibitor of HIV-1.Journal of virology · 2016Article
- Inhibitor-Based Therapeutics for Treatment of Viral Hepatitis.Journal of clinical and translational hepatology · 2016Review
- Viral channel forming proteins--How to assemble and depolarize lipid membranes in silico.Biochimica et biophysica acta · 2016Review
- Targeting the Channel Activity of Viroporins.Advances in protein chemistry and structural biology · 2016Review
- Characterising protein/detergent complexes by triple-detection size-exclusion chromatography.Biological procedures online · 2016Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
HIV-1 Vpu is an 81-residue protein with a single N-terminal transmembrane (TM) helical segment that is involved in the release of new virions from host cell membranes. Vpu and its TM segment form ion channels in phospholipid bilayers, presumably by oligomerization of TM helices into a pore-like structure. We describe measurements that provide new constraints on the oligomerization state and supramolecular structure of residues 1-40 of Vpu (Vpu(1-40)), including analytical ultracentrifugation measurements to investigate oligomerization in detergent micelles, photo-induced crosslinking experiments to investigate oligomerization in bilayers, and solid-state nuclear magnetic resonance measurements to obtain constraints on intermolecular contacts between and orientations of TM helices in bilayers. From these data, we develop molecular models for Vpu TM oligomers. The data indicate that a variety of oligomers coexist in phospholipid bilayers, so that a unique supramolecular structure can not be defined. Nonetheless, since oligomers of various sizes have similar intermolecular contacts and orientations, molecular models developed from our data are most likely representative of Vpu TM oligomers that exist in host cell membranes.
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