ArticleeLife2025
Ab initio prediction of specific phospholipid complexes and membrane association of HIV-1 MPER antibodies by multi-scale simulations.
Article in eLife, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The trial behind it
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Who cites it
5 citing papers in PubMed.
- Structural basis of membrane engagement and polyreactivity control in HIV-1 MPER broadly neutralizing antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- In Vitro Selection of Antibodies TargetingPathogens (Basel, Switzerland) · 2026Article
- Probing the role of membrane in neutralizing activity of antibodies against influenza virus.Structure (London, England : 1993) · 2026Article
- Cryo-EM structures of antibodies elicited by germline-targeting HIV MPER epitope scaffolds.Cell reports · 2026Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
A potent class of HIV-1 broadly neutralizing antibodies (bnAbs) targets the envelope glycoprotein's membrane proximal exposed region (MPER) through a proposed mechanism where hypervariable loops embed into lipid bilayers and engage headgroup moieties alongside the epitope. We address the feasibility and determinant molecular features of this mechanism using multi-scale modeling. All-atom simulations of 4E10, PGZL1, 10E8, and LN01 docked onto HIV-like membranes consistently form phospholipid complexes at key complementarity-determining region loop sites, solidifying that stable and specific lipid interactions anchor bnAbs to membrane surfaces. Ancillary protein-lipid contacts reveal surprising contributions from antibody framework regions. Coarse-grained simulations effectively capture antibodies embedding into membranes. Simulations estimating protein-membrane interaction strength for PGZL1 variants along an inferred maturation pathway show bilayer affinity is evolved and correlates with neutralization potency. The modeling demonstrated here uncovers insights into lipid participation in antibodies' recognition of membrane proteins and highlights antibody features to prioritize in vaccine design.
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Registered trials
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