ArticleThe Journal of clinical investigation2015
Redesigned HIV antibodies exhibit enhanced neutralizing potency and breadth.
Article in The Journal of clinical investigation, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- Genotypic challenges in implementing broadly neutralizing antibody-based long-acting HIV-1 therapies.Communications medicine · 2026Review
- Enabling the immune escaped etesevimab fully-armed against SARS-CoV-2 Omicron subvariants including KP.2.hLife · 2025Article
- High-throughput analysis system of interaction kinetics for data-driven antibody design.Scientific reports · 2023Article
- Improved HIV-1 neutralization breadth and potency of V2-apex antibodies by in silico design.Cell reports · 2023Article
- Guiding protein design choices by per-residue energy breakdown analysis with an interactive web application.Frontiers in molecular biosciences · 2023Article
- Tyrosine O-sulfation proteoforms affect HIV-1 monoclonal antibody potency.Scientific reports · 2022Article
- Charged Residue Implantation Improves the Affinity of a Cross-Reactive Dengue Virus Antibody.International journal of molecular sciences · 2022Article
- Article
- An expanded benchmark for antibody-antigen docking and affinity prediction reveals insights into antibody recognition determinants.Structure (London, England : 1993) · 2021Article
- Modeling Immunity with Rosetta: Methods for Antibody and Antigen Design.Biochemistry · 2021Review
- Antibodies targeting epitopes on the cell-surface form of NS1 protect against Zika virus infection during pregnancy.Nature communications · 2020Article
- Effects of a remote mutation from the contact paratope on the structure of CDR-H3 in the anti-HIV neutralizing antibody PG16.Scientific reports · 2019Article
- A generalized HIV vaccine design strategy for priming of broadly neutralizing antibody responses.Science (New York, N.Y.) · 2019Article
- Role of antibody heavy and light chain interface residues in affinity maturation of binding to HIV envelope glycoprotein.Molecular systems design & engineering · 2019Article
- Selection of immunoglobulin elbow region mutations impacts interdomain conformational flexibility in HIV-1 broadly neutralizing antibodies.Nature communications · 2019Article
- Multistate design of influenza antibodies improves affinity and breadth against seasonal viruses.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural Diversity of Ultralong CDRH3s in Seven Bovine Antibody Heavy Chains.Frontiers in immunology · 2019Article
- Integrating linear optimization with structural modeling to increase HIV neutralization breadth.PLoS computational biology · 2018Article
- Principles of Broad and Potent Antiviral Human Antibodies: Insights for Vaccine Design.Cell host & microbe · 2017Review
- Engineering broadly neutralizing antibodies for HIV prevention and therapy.Advanced drug delivery reviews · 2016Review
Corrections and comments
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
Abstract
Several HIV envelope-targeting (Env-targeting) antibodies with broad and potent neutralizing activity have been identified and shown to have unusual features. Of these, the PG9 antibody has a long heavy chain complementarity determining region 3 (HCDR3) and possesses unique structural elements that interact with protein and glycan features of the HIV Env glycoprotein. Here, we used the Rosetta software suite to design variants of the PG9 antibody HCDR3 loop with the goal of identifying variants with increased potency and breadth of neutralization for diverse HIV strains. One variant, designated PG9_N100(F)Y, possessed increased potency and was able to neutralize a diverse set of PG9-resistant HIV strains, including those lacking the Env N160 glycan, which is critical for PG9 binding. An atomic resolution structure of the PG9_N100(F)Y fragment antigen binding (Fab) confirmed that the mutated residue retains the paratope surface when compared with WT PG9. Differential scanning calorimetry experiments revealed that the mutation caused a modest increase in thermodynamic stability of the Fab, a feature predicted by the computational model. Our findings suggest that thermodynamic stabilization of the long HCDR3 in its active conformation is responsible for the increased potency of PG9_N100(F)Y, and strategies aimed at stabilizing this region in other HIV antibodies could become an important approach to in silico optimization of antibodies.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.