ArticleProceedings of the National Academy of Sciences of the United States of America2010
Prolonged exposure of the HIV-1 gp41 membrane proximal region with L669S substitution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Infectious virion capture by HIV-1 gp120-specific IgG from RV144 vaccinees.Journal of virology · 2013Trial
- Current Approaches for Assessments of Neutralizing, Binding, and Effector Functions of Antibodies on the Path to Antibody-Mediated Prevention Strategies for HIV-1.Current HIV research · 2026Review
- An HIV-1 gp41 peptide-liposome vaccine elicits neutralizing epitope-targeted antibody responses in healthy individuals.medRxiv : the preprint server for health sciences · 2025Article
- Parameter estimation and identifiability analysis for a bivalent analyte model of monoclonal antibody-antigen binding.Analytical biochemistry · 2023Article
- Global Increases in Human Immunodeficiency Virus Neutralization Sensitivity Due to Alterations in the Membrane-Proximal External Region of the Envelope Glycoprotein Can Be Minimized by Distant State 1-Stabilizing Changes.Journal of virology · 2022Article
- Autoreactivity and broad neutralization of antibodies against HIV-1 are governed by distinct mutations: Implications for vaccine design strategies.Frontiers in immunology · 2022Article
- Antibody response against selected epitopes in the HIV-1 envelope gp41 ectodomain contributes to reduce viral burden in HIV-1 infected patients.Scientific reports · 2021Article
- Article
- Unique genotypic features of HIV-1 C gp41 membrane proximal external region variants during pregnancy relate to mother-to-child transmission via breastfeeding.Journal of clinical pediatrics and neonatology · 2021Article
- Geospatial HIV-1 subtype C gp120 sequence diversity and its predicted impact on broadly neutralizing antibody sensitivity.PloS one · 2021Article
- Neutralizing Antibodies Targeting HIV-1 gp41.Viruses · 2020Review
- Gp41-targeted antibodies restore infectivity of a fusion-deficient HIV-1 envelope glycoprotein.PLoS pathogens · 2020Article
- Structural Basis for Broad HIV-1 Neutralization by the MPER-Specific Human Broadly Neutralizing Antibody LN01.Cell host & microbe · 2019Article
- Structure of the membrane proximal external region of HIV-1 envelope glycoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Molecular Basis of Unusually High Neutralization Resistance in Tier 3 HIV-1 Strain 253-11.Journal of virology · 2018Article
- Potent and broad HIV-neutralizing antibodies in memory B cells and plasma.Science immunology · 2017Article
- Amino Acid Changes in the HIV-1 gp41 Membrane Proximal Region Control Virus Neutralization Sensitivity.EBioMedicine · 2016Article
- Enhanced antibody-mediated neutralization of HIV-1 variants that are resistant to fusion inhibitors.Retrovirology · 2016Article
- Initiation of immune tolerance-controlled HIV gp41 neutralizing B cell lineages.Science translational medicine · 2016Article
- Human Non-neutralizing HIV-1 Envelope Monoclonal Antibodies Limit the Number of Founder Viruses during SHIV Mucosal Infection in Rhesus Macaques.PLoS pathogens · 2015Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
The conserved membrane-proximal external region (MPER) of HIV-1 envelope is a target for the rare broadly neutralizing 2F5, Z13, and 4E10 monoclonal antibodies (mAbs). One strategy to elicit such antibodies is to design an immunogen with increased exposure of the 2F5 and 4E10 mAb epitopes. In this study we characterize a single leucine to serine substitution at position 669 (L669S) in the gp41 Env MPER that confers >250-fold more neutralization sensitivity to 2F5 and 4E10 mAbs than does the wild-type gp41 sequence. On synthetic liposomes, increased solvent exposure of MPER tryptophan residues and stable docking of 2F5 and 4E10 mAbs to mutant MPER peptide liposomes indicate more favorable membrane orientation of MPER neutralizing epitopes with L669S substitution. The time during which virus is sensitive to 2F5 mAb-mediated neutralization is approximately 3-fold longer when the mutation is present. These data suggest that a major contribution to the L669S mutant virus phenotype of enhanced susceptibility to MPER mAbs is prolonged exposure of the MPER neutralizing epitope during viral entry.
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