ArticleNature communications2021
Distinct conformations of the HIV-1 V3 loop crown are targetable for broad neutralization.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Structural determination of the HIV-1 Variable Region 3 epitope of antibody 19b.Journal of virology · 2026Article
- Glycan-reactive antibodies isolated from human HIV-1 vaccine trial participants show broad pathogen cross-reactivity.Journal of virology · 2025Article
- A high temperature responsive UDP-glucosyltransferase gene OsUGT72F1 enhances heat tolerance in rice and Arabidopsis.Plant cell reports · 2025Article
- Structure-based design of an immunogenic, conformationally stabilized FimH antigen for a urinary tract infection vaccine.PLoS pathogens · 2025Article
- Assessing bnAb potency in the context of HIV-1 envelope conformational plasticity.PLoS pathogens · 2025Article
- Beyond glycan barriers: non-cognate ligands and protein mimicry approaches to elicit broadly neutralizing antibodies for HIV-1.Journal of biomedical science · 2024Review
- Assessing immunogenicity barriers of the HIV-1 envelope trimer.NPJ vaccines · 2023Article
- Broadly neutralizing antibody epitopes on HIV-1 particles are exposed after virus interaction with host cells.Journal of virology · 2023Article
- Conserved HIV-1 V3 loop helix offers potential for broad neutralization.Nature structural & molecular biology · 2023Article
- Trapping the HIV-1 V3 loop in a helical conformation enables broad neutralization.Nature structural & molecular biology · 2023Article
- Designed Ankyrin Repeat Proteins as a tool box for analyzing p63.Cell death and differentiation · 2022Article
- Review
- Neutralizing Antibodies Against Allosteric Proteins: Insights From a Bacterial Adhesin.Journal of molecular biology · 2022Review
- Neutralization Sensitivity of HIV-1 CRF07_BC From an Untreated Patient With a Focus on Evolution Over Time.Frontiers in cellular and infection microbiology · 2022Article
Corrections and comments
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Authors and funding
25 authors at 5 institutions in 6 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The V3 loop of the HIV-1 envelope (Env) protein elicits a vigorous, but largely non-neutralizing antibody response directed to the V3-crown, whereas rare broadly neutralizing antibodies (bnAbs) target the V3-base. Challenging this view, we present V3-crown directed broadly neutralizing Designed Ankyrin Repeat Proteins (bnDs) matching the breadth of V3-base bnAbs. While most bnAbs target prefusion Env, V3-crown bnDs bind open Env conformations triggered by CD4 engagement. BnDs achieve breadth by focusing on highly conserved residues that are accessible in two distinct V3 conformations, one of which resembles CCR5-bound V3. We further show that these V3-crown conformations can, in principle, be attacked by antibodies. Supporting this conclusion, analysis of antibody binding activity in the Swiss 4.5 K HIV-1 cohort (n = 4,281) revealed a co-evolution of V3-crown reactivities and neutralization breadth. Our results indicate a role of V3-crown responses and its conformational preferences in bnAb development to be considered in preventive and therapeutic approaches.
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