ArticleBiophysical journal2013
Membrane structure correlates to function of LLP2 on the cytoplasmic tail of HIV-1 gp41 protein.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 23 citations in OpenAlex.
- HIV-1 Env Heterogeneity: Cleavage, Trafficking, and Antigenic Consequences for Virions and Infected Cells.Viruses · 2026Review
- Novel Helical Trp- and Arg-Rich Antimicrobial Peptides Locate Near Membrane Surfaces and Rigidify Lipid Model Membranes.Advanced nanobiomed research · 2023Article
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- Changes in membrane elasticity caused by the hydrophobic surfactant proteins correlate poorly with adsorption of lipid vesicles.Soft matter · 2021Article
- Scaling relationships for the elastic moduli and viscosity of mixed lipid membranes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Efficiently cleaved HIV-1 envelopes: can they be important for vaccine immunogen development?Therapeutic advances in vaccines and immunotherapy · 2020Review
- Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers.Soft matter · 2019Article
- Cell surface ectodomain integrity of a subset of functional HIV-1 envelopes is dependent on a conserved hydrophilic domain containing region in their C-terminal tail.Retrovirology · 2018Article
- Physics of HIV.Journal of physics D: Applied physics · 2018Article
- Selective Interaction of Colistin with Lipid Model Membranes.Biophysical journal · 2018Article
- Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein.Structure (London, England : 1993) · 2017Article
- HIV-1 matrix-31 membrane binding peptide interacts differently with membranes containing PS vs. PI(4,5)PBiochimica et biophysica acta · 2016Article
- Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein.Biochimica et biophysica acta · 2016Review
- Determination of mosaicity in oriented stacks of lipid bilayers.Soft matter · 2016Article
- Fusion-competent state induced by a C-terminal HIV-1 fusion peptide in cholesterol-rich membranes.Biochimica et biophysica acta · 2015Article
- The cytoplasmic tail of retroviral envelope glycoproteins.Progress in molecular biology and translational science · 2015Review
- HIV-1 Tat membrane interactions probed using X-ray and neutron scattering, CD spectroscopy and MD simulations.Biochimica et biophysica acta · 2014Article
- Life at the border: adaptation of proteins to anisotropic membrane environment.Protein science : a publication of the Protein Society · 2014Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Mutation studies previously showed that the lentivirus lytic peptide (LLP2) sequence of the cytoplasmic C-terminal tail of the HIV-1 gp41 envelope protein inhibited viral-initiated T-cell death and T-cell syncytium formation, at which time in the HIV life cycle the gp41 protein is embedded in the T-cell membrane. In striking contrast, the mutants did not affect virion infectivity, during which time the gp41 protein is embedded in the HIV envelope membrane. To examine the role of LLP2/membrane interactions, we applied synchrotron x-radiation to determine structure of hydrated membranes. We focused on WT LLP2 peptide (+3 charge) and MX2 mutant (-1 charge) with membrane mimics for the T-cell and the HIV-1 membranes. To investigate the influence of electrostatics, cholesterol content, and peptide palmitoylation, we also studied three other LLP2 variants and HIV-1 mimics without negatively charged lipids or cholesterol as well as extracted HIV-1 lipids. All LLP2 peptides bound strongly to T-cell membrane mimics, as indicated by changes in membrane structure and bending. In contrast, none of the weakly bound LLP2 variants changed the HIV-1 membrane mimic structure or properties. This correlates well with, and provides a biophysical basis for, previously published results that reported lack of a mutant effect in HIV virion infectivity in contrast to an inhibitory effect in T-cell syncytium formation. It shows that interaction of LLP2 with the T-cell membrane modulates biological function.
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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.