ArticlePloS one2017
Peptide Targeted by Human Antibodies Associated with HIV Vaccine-Associated Protection Assumes a Dynamic α-Helical Structure.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The RV144 Trial Might Still Yield Useful Information.Current HIV research · 2026Review
- Broadly neutralizing antibody epitopes on HIV-1 particles are exposed after virus interaction with host cells.Journal of virology · 2023Article
- Cholera toxin B scaffolded, focused SIV V2 epitope elicits antibodies that influence the risk of SIVFrontiers in immunology · 2023Article
- Differential V2-directed antibody responses in non-human primates infected with SHIVs or immunized with diverse HIV vaccines.Nature communications · 2022Article
- Anti-V2 antibodies virus vulnerability revealed by envelope V1 deletion in HIV vaccine candidates.iScience · 2021Article
- An HIV Vaccine Targeting the V2 Region of the HIV Envelope Induces a Highly Durable Polyfunctional Fc-Mediated Antibody Response in Rhesus Macaques.Journal of virology · 2020Article
- Article
- Unbiased Identification of Immunogenic Staphylococcus aureus Leukotoxin B-Cell Epitopes.Infection and immunity · 2020Article
- Multimeric Epitope-Scaffold HIV Vaccines Target V1V2 and Differentially Tune Polyfunctional Antibody Responses.Cell reports · 2019Article
- Humoral Response to the HIV-1 Envelope V2 Region in a Thai Early Acute Infection Cohort.Cells · 2019Article
- Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions.Nature communications · 2018Article
- Select gp120 V2 domain specific antibodies derived from HIV and SIV infection and vaccination inhibit gp120 binding to α4β7.PLoS pathogens · 2018Article
- Fasciola spp: Mapping of the MF6 epitope and antigenic analysis of the MF6p/HDM family of heme-binding proteins.PloS one · 2017Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The only evidence of vaccine-induced protection from HIV acquisition in humans was obtained in the RV144 HIV vaccine clinical trial. One immune correlate of risk in RV144 was observed to be higher titers of vaccine-induced antibodies (Abs) reacting with a 23-mer non-glycosylated peptide with the same amino acid sequence as a segment in the second variable (V2) loop of the MN strain of HIV. We used NMR to analyze the dynamic 3D structure of this peptide. Distance restraints between spatially proximate inter-residue protons were calculated from NOE cross peak intensities and used to constrain a thorough search of all possible conformations of the peptide. α-helical folding was strongly preferred by part of the peptide. A high-throughput structure prediction of this segment in all circulating HIV strains demonstrated that α-helical conformations are preferred by this segment almost universally across all subtypes. Notably, α-helical conformations of this segment of the V2 loop cluster cross-subtype-conserved amino acids on one face of the helix and the variable amino acid positions on the other in a semblance of an amphipathic α-helix. Accordingly, some Abs that protected against HIV in RV144 may have targeted a specific, conserved α-helical peptide epitope in the V2 loop of HIV's surface envelope glycoprotein.
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