ArticleBiophysical journal2003
Structural and functional roles of HIV-1 gp41 pretransmembrane sequence segmentation.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Structural and functional analyses of viral H2 protein of the vaccinia virus entry fusion complex.Journal of virology · 2023Article
- Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope.Communications biology · 2022Article
- The endoplasmic reticulum proteostasis network profoundly shapes the protein sequence space accessible to HIV envelope.PLoS biology · 2022Article
- 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
- Effects of HIV-1 gp41-Derived Virucidal Peptides on Virus-like Lipid Membranes.Biophysical journal · 2017Article
- Insights into vaccine development for acquired immune deficiency syndrome from crystal structures of human immunodeficiency virus-1 gp41 and equine infectious anemia virus gp45.Protein science : a publication of the Protein Society · 2015Review
- The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and Its Connection to the Immunogenic Membrane-proximal External Region.The Journal of biological chemistry · 2015Article
- Fusion-competent state induced by a C-terminal HIV-1 fusion peptide in cholesterol-rich membranes.Biochimica et biophysica acta · 2015Article
- Article
- The three lives of viral fusion peptides.Chemistry and physics of lipids · 2014Review
- Forced virus evolution reveals functional crosstalk between the disulfide bonded region and membrane proximal ectodomain region of HIV-1 gp41.Retrovirology · 2013Article
- Mechanism of membrane perturbation by the HIV-1 gp41 membrane-proximal external region and its modulation by cholesterol.Biochimica et biophysica acta · 2012Article
- Role for the terminal clasp of HIV-1 gp41 glycoprotein in the initiation of membrane fusion.The Journal of biological chemistry · 2011Article
- Membrane-proximal external HIV-1 gp41 motif adapted for destabilizing the highly rigid viral envelope.Biophysical journal · 2011Article
- Membrane topology analysis of HIV-1 envelope glycoprotein gp41.Retrovirology · 2010Article
- Cholesterol-binding viral proteins in virus entry and morphogenesis.Sub-cellular biochemistry · 2010Review
- Mutagenesis of the transmembrane domain of the SARS coronavirus spike glycoprotein: refinement of the requirements for SARS coronavirus cell entry.Virology journal · 2009Article
- Stable docking of neutralizing human immunodeficiency virus type 1 gp41 membrane-proximal external region monoclonal antibodies 2F5 and 4E10 is dependent on the membrane immersion depth of their epitope regions.Journal of virology · 2009Article
- Structure of the HIV-1 gp41 membrane-proximal ectodomain region in a putative prefusion conformation.Biochemistry · 2009Article
- Identification of the LWYIK motif located in the human immunodeficiency virus type 1 transmembrane gp41 protein as a distinct determinant for viral infection.Journal of virology · 2009Article
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Authors and funding
7 authors.
Funding
Abstract
The membrane-proximal segment connecting the helical core with the transmembrane anchor of human immunodeficiency virus type 1 gp41 is accessible to broadly neutralizing antibodies and plays a crucial role in fusion activity. New predictive approaches including computation of interfacial affinity and the corresponding hydrophobic moments suggest that this region is functionally segmented into two consecutive subdomains: one amphipathic at the N-terminal side and one fully interfacial at the C-terminus. The N-terminal subdomain would extend alpha-helices from the preceding carboxy-terminal heptad repeat and provide, at the same time, a hydrophobic-at-interface surface. Experiments were performed to compare a wild-type representing pretransmembrane peptide with a nonamphipathic defective sequence, which otherwise conserved interfacial hydrophobicity at the carboxy-subdomain. Results confirmed that both penetrated equally well into lipid monolayers and both were able to partition into membrane interfaces. However only the functional sequence: 1), adopted helical structures in solution and in membranes; 2), formed homo-oligomers in solution and membranes; and 3), inhibited gp41-induced cell-cell fusion. These data support two roles for gp41 aromatic-rich pretransmembrane sequence: 1), oligomerization of gp41; and 2), immersion into the viral membrane interface. Accessibility to membrane interfaces and subsequent adoption of the low-energy structure may augment helical bundle formation and perhaps be related to a concomitant loss of immunoreactivity. These results may have implications in the development of HIV-1 fusion inhibitors and vaccines.
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