ArticleProceedings of the National Academy of Sciences of the United States of America2012
HIV-1 Gag protein can sense the cholesterol and acyl chain environment in model membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 106 citations in OpenAlex.
- Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication.FEMS microbiology reviews · 2026Review
- Non-AUG HIV-1 uORF translation elicits specific T cell immune response and regulates viral transcript expression.Nature communications · 2025Article
- The Assembly of HTLV-1-How Does It Differ from HIV-1?Viruses · 2024Review
- HIV-1 Gag Polyprotein Affinity to the Lipid Membrane Is Independent of Its Surface Charge.Biomolecules · 2024Article
- Human Immunodeficiency Virus Type 1 Gag Polyprotein Modulates Membrane Physical Properties like a Surfactant: Potential Implications for Virus Assembly.ACS infectious diseases · 2024Article
- Sorting of complex sphingolipids within the cellular endomembrane systems.Frontiers in cell and developmental biology · 2024Review
- HIV-1 Gag targeting to the plasma membrane reorganizes sphingomyelin-rich and cholesterol-rich lipid domains.Nature communications · 2023Article
- Understanding the free-energy landscape of phase separation in lipid bilayers using molecular dynamics.Biophysical journal · 2023Article
- Understanding the Free Energy Landscape of Phase Separation in Lipid Bilayers using Molecular Dynamics.bioRxiv : the preprint server for biology · 2023Article
- Inhibition of neutral sphingomyelinase 2 impairs HIV-1 envelope formation and substantially delays or eliminates viral rebound.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Thermoplasmonic Vesicle Fusion Reveals Membrane Phase Segregation of Influenza Spike Proteins.Nano letters · 2023Article
- Atomic view of the HIV-1 matrix lattice; implications on virus assembly and envelope incorporation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Review
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- Structural Insights into the Mechanism of Human T-cell Leukemia Virus Type 1 Gag Targeting to the Plasma Membrane for Assembly.Journal of molecular biology · 2021Article
- Methods for Studying Endocytotic Pathways of Herpesvirus Encoded G Protein-Coupled Receptors.Molecules (Basel, Switzerland) · 2020Review
- Lateral heterogeneity and domain formation in cellular membranes.Chemistry and physics of lipids · 2020Article
- Mechanisms of PI(4,5)P2 Enrichment in HIV-1 Viral Membranes.Journal of molecular biology · 2020Article
- Liposome-Based Bioassays.Biology · 2020Review
12 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Membrane binding of the HIV-1 group-specific antigen (Gag) structural protein, a critical step in viral assembly at the plasma membrane, is mediated by the myristoylated, highly basic matrix (MA) domain, which interacts with negatively charged lipids in the inner leaflet. According to a popular model, virus particles bud from membrane rafts, microdomains enriched in cholesterol and high-melting phospholipids with higher order than found outside rafts. How Gag might recognize membrane rafts, if they exist in the inner leaflet, is unknown. Using a liposome flotation assay with proteins translated in vitro, we investigated whether Gag can sense the composition of the hydrophobic part of the bilayer, by fixing lipid head group composition and varying hydrophobic properties. In liposomes composed solely of phosphatidylserine and phosphatidylcholine, and with the same overall membrane negative charge, Gag strongly preferred lipids with both acyl chains unsaturated over those with only one chain unsaturated. Adding cholesterol increased Gag binding and led to closer packing of phospholipids. However, higher membrane order, as measured by electron spin resonance, was not correlated with increased Gag binding. Gag proteins from two other retroviruses gave similar results. These liposome binding preferences were qualitatively recapitulated by purified myristoylated HIV-1 MA. Phosphatidylinositol 4,5-bisphosphate and cholesterol enhanced binding in an additive manner. Taken together, these results show that Gag is sensitive both to the acyl chains of phosphatidylserine and to cholesterol concentration and other details of the membrane environment. These observations may help explain how retroviruses acquire a raft-like lipid composition.
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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.