ArticleJournal of molecular biology2013
Rapid conformational epitope mapping of anti-gp120 antibodies with a designed mutant panel displayed on yeast.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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.
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Who cites it
40 citing papers in PubMed, 65 citations in OpenAlex.
- Boosting of HIV envelope CD4 binding site antibodies with long variable heavy third complementarity determining region in the randomized double blind RV305 HIV-1 vaccine trial.PLoS pathogens · 2017Trial
- Egyptian rousette bat humoral immunity to H9 influenza hemagglutinin.bioRxiv : the preprint server for biology · 2026Article
- Human naïve B cells recognize prepandemic influenza virus hemagglutinins.Science immunology · 2025Article
- Rapid Mapping of Protein Binding Sites and Conformational Epitopes by Coupling Yeast Surface Display to Chemical Labeling and Deep Sequencing.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Engineered TIMP2 with narrow MMP-9 specificity is an effective inhibitor of invasion and proliferation of triple-negative breast cancer cells.The Journal of biological chemistry · 2024Article
- Deep neural networks for predicting the affinity landscape of protein-protein interactions.iScience · 2024Article
- Crimean-Congo hemorrhagic fever survivors elicit protective non-neutralizing antibodies that target 11 overlapping regions on glycoprotein GP38.Cell reports · 2024Article
- A library-on-library screen reveals the breadth expansion landscape of a broadly neutralizing betacoronavirus antibody.bioRxiv : the preprint server for biology · 2024Article
- Crimean-Congo Hemorrhagic Fever Survivors Elicit Protective Non-Neutralizing Antibodies that Target 11 Overlapping Regions on Viral Glycoprotein GP38.bioRxiv : the preprint server for biology · 2024Article
- Mutational scan inferred binding energetics and structure in intrinsically disordered protein CcdA.Protein science : a publication of the Protein Society · 2023Article
- Article
- Yeast Surface Display for Protein Engineering: Library Generation, Screening, and Affinity Maturation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- A Protein-Engineered, Enhanced Yeast Display Platform for Rapid Evolution of Challenging Targets.ACS synthetic biology · 2021Article
- Naive human B cells engage the receptor binding domain of SARS-CoV-2, variants of concern, and related sarbecoviruses.Science immunology · 2021Article
- Protective neutralizing antibodies from human survivors of Crimean-Congo hemorrhagic fever.Cell · 2021Article
- Noncompetitive Allosteric Antagonism of Death Receptor 5 by a Synthetic Affibody Ligand.Biochemistry · 2020Article
- Quantitative mapping of binding specificity landscapes for homologous targets by using a high-throughput method.The Biochemical journal · 2020Article
- Integration of phage and yeast display platforms: A reliable and cost effective approach for binning of peptides as displayed on-phage.PloS one · 2020Article
- Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition.The Journal of biological chemistry · 2019Article
- Identification of variant HIV envelope proteins with enhanced affinities for precursors to anti-gp41 broadly neutralizing antibodies.PloS one · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
gp120 is a substrate for protein engineering both for human immunodeficiency virus (HIV) immunogen design and as a bait for isolating anti-HIV antibodies from patient samples. In this work, we describe the display of a stripped core gp120 on the yeast cell surface. Validation against a panel of neutralizing antibodies confirms that yeast-displayed gp120 presents the CD4 binding site in the correct conformation. We map the epitope of the broadly neutralizing anti-gp120 antibody VRC01 using both a random mutagenesis library and a defined mutant panel and find that the resultant epitope maps are consistent with one another and with the crystallographically identified contact residues. Mapping the VRC01-competitive antibodies b12 and b13 reveals energetic differences in their epitopes that are not obvious from existing crystal structures. These data suggest mutation sets that abrogate binding to broadly neutralizing antibodies with greater specificity than the canonical mutation D368R, useful in rapidly assessing the nature of a vaccine response.
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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.