ArticleCell reports2018
Surface-Matrix Screening Identifies Semi-specific Interactions that Improve Potency of a Near Pan-reactive HIV-1-Neutralizing Antibody.
Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
What it found
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Who cites it
52 citing papers in PubMed, 72 citations in OpenAlex.
- 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
- Genotypic challenges in implementing broadly neutralizing antibody-based long-acting HIV-1 therapies.Communications medicine · 2026Review
- Probing the role of membrane in neutralizing activity of antibodies against influenza virus.Structure (London, England : 1993) · 2026Article
- Antibody-drug conjugates for infectious and neglected tropical diseases: chemical design principles, target biology, and translational challenges.Frontiers in chemistry · 2026Review
- Transient glycan shield reduction induces CD4-binding site broadly neutralizing antibodies in SHIV-infected macaques.Cell reports · 2025Article
- Distinctive Membrane Accommodation Traits Underpinning the Neutralization Activity of HIV-1 Antibody against MPER.Molecular pharmaceutics · 2025Article
- Engineering of CD8mBio · 2025Article
- Article
- Structural development of the HIV-1 apex-directed PGT145-PGDM1400 antibody lineage.Cell reports · 2025Article
- Defining criteria for broadly neutralizing HIV antibodies.Frontiers in immunology · 2025Review
- Generation of a Nonbilayer Lipid Nanoenvironment after Epitope Binding Potentiates Neutralizing HIV-1 MPER Antibody.ACS applied materials & interfaces · 2024Article
- Design of soluble HIV-1 envelope trimers free of covalent gp120-gp41 bonds with prevalent native-like conformation.Cell reports · 2024Article
- Cholesterol reduction by immunization with a PCSK9 mimic.Cell reports · 2024Article
- Phase 1 trial evaluating safety and pharmacokinetics of HIV-1 broadly neutralizing mAbs 10E8VLS and VRC07-523LS.JCI insight · 2024Article
- Cleavage-intermediate Lassa virus trimer elicits neutralizing responses, identifies neutralizing nanobodies, and reveals an apex-situated site-of-vulnerability.Nature communications · 2024Article
- Vaccine-elicited and naturally elicited antibodies differ in their recognition of the HIV-1 fusion peptide.Frontiers in immunology · 2024Article
- Article
- HIV-1 neutralizing antibodies elicited in humans by a prefusion-stabilized envelope trimer form a reproducible class targeting fusion peptide.Cell reports · 2023Article
- Improved HIV-1 neutralization breadth and potency of V2-apex antibodies by in silico design.Cell reports · 2023Article
- Quantitative characterization of membrane-protein reversible association using FCS.Biophysical journal · 2023Article
Corrections and comments
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Authors and funding
33 authors at 4 institutions in 1 country.
Funding
Abstract
Highly effective HIV-1-neutralizing antibodies could have utility in the prevention or treatment of HIV-1 infection. To improve the potency of 10E8, an antibody capable of near pan-HIV-1 neutralization, we engineered 10E8-surface mutants and screened for improved neutralization. Variants with the largest functional enhancements involved the addition of hydrophobic or positively charged residues, which were positioned to interact with viral membrane lipids or viral glycan-sialic acids, respectively. In both cases, the site of improvement was spatially separated from the region of antibody mediating molecular contact with the protein component of the antigen, thereby improving peripheral semi-specific interactions while maintaining unmodified dominant contacts responsible for broad recognition. The optimized 10E8 antibody, with mutations to phenylalanine and arginine, retained the extraordinary breadth of 10E8 but with ∼10-fold increased potency. We propose surface-matrix screening as a general method to improve antibodies, with improved semi-specific interactions between antibody and antigen enabling increased potency without compromising breadth.
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