ArticleBiochemistry2010
Major antiparallel and minor parallel β sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide.
Article in Biochemistry, 2010. 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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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Very broad distribution of β sheet registries of the HIV gp41 fusion peptide supports mutational robustness for fusion and infection.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Lipid acyl chain protrusion induced by the influenza virus hemagglutinin fusion peptide detected by NMR paramagnetic relaxation enhancement.Biophysical chemistry · 2023Article
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- UV Resonance Raman explores protein structural modification upon fibrillation and ligand interaction.Biophysical journal · 2021Article
- Article
- RapidBiochemistry · 2021Article
- Article
- Membrane Composition Modulates Fusion by Altering Membrane Properties and Fusion Peptide Structure.The Journal of membrane biology · 2019Review
- Structure and Dynamics of Membrane Proteins from Solid-State NMR.Annual review of biophysics · 2018Review
- Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains.Biochemistry · 2018Article
- Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion Catalysis.Journal of the American Chemical Society · 2015Article
- Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
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- The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.The Journal of biological chemistry · 2015Article
- Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle state.Journal of molecular biology · 2014Article
- HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion.Biophysical journal · 2014Article
- Solid-state nuclear magnetic resonance measurements of HIV fusion peptide 13CO to lipid 31P proximities support similar partially inserted membrane locations of the α helical and β sheet peptide structures.The journal of physical chemistry. A · 2013Article
- Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.Journal of biomolecular NMR · 2013Article
- Computer-Aided Approaches for Targeting HIVgp41.Biology · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The HIV gp41 protein catalyzes fusion between viral and host cell membranes, and its apolar N-terminal region or "fusion peptide" binds to the host cell membrane and plays a key role in fusion. "HFP" is a construct containing the fusion peptide sequence, induces membrane vesicle fusion, and is an important fusion model system. Earlier solid-state nuclear magnetic resonance (SSNMR) studies showed that when HFP is associated with membranes with ∼30 mol % cholesterol, the first 16 residues have predominant β strand secondary structure and a fraction of the strands form antiparallel β sheet structure with residue 16→1/1→16 or 17→1/1→17 registries for adjacent strands. In some contrast, other SSNMR and infrared studies have been interpreted to support a large fraction of an approximately in-register parallel registry of adjacent strands. However, the samples had extensive isotopic labeling, and other structural models were also consistent with the data. This SSNMR study uses sparse labeling schemes that reduce ambiguity in the determination of the fraction of HFP molecules with parallel β registry. Quantitative analysis of the data shows that the parallel fraction is at most 0.15 with a much greater fraction of antiparallel 16→1/1→16 and 17→1/1→17 registries. These data strongly support a model of HFP-induced vesicle fusion caused by antiparallel rather than parallel registries and provide insight into the arrangement of gp41 molecules during HIV-host cell fusion. This study is an example of quantitative determination of a complex structural distribution by SSNMR, including experimentally validated inclusion of natural abundance contributions to the SSNMR data.
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