ArticlePLoS pathogens2009
Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site.
Article in PLoS pathogens, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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Who cites it
89 citing papers in PubMed, 118 citations in OpenAlex.
- Longitudinal dynamics of the HIV-specific B cell response during intermittent treatment of primary HIV infection.PloS one · 2017Trial
- Review
- Reconstruction of a polyclonal ADCC antibody repertoire from an HIV-1 non-transmitting mother.iScience · 2023Article
- Glycan masking in vaccine design: Targets, immunogens and applications.Frontiers in immunology · 2023Review
- In vivo engineered B cells secrete high titers of broadly neutralizing anti-HIV antibodies in mice.Nature biotechnology · 2022Article
- Designing and characterization of a SARS-CoV-2 immunogen with receptor binding motif grafted on a protein scaffold: An epitope-focused vaccine approach.International journal of biological macromolecules · 2022Article
- Review
- Structural basis of glycan276-dependent recognition by HIV-1 broadly neutralizing antibodies.Cell reports · 2021Article
- CD4+ T Cells Are Dispensable for Induction of Broad Heterologous HIV Neutralizing Antibodies in Rhesus Macaques.Frontiers in immunology · 2021Article
- Automated Design by Structure-Based Stabilization and Consensus Repair to Achieve Prefusion-Closed Envelope Trimers in a Wide Variety of HIV Strains.Cell reports · 2020Article
- Gp41-targeted antibodies restore infectivity of a fusion-deficient HIV-1 envelope glycoprotein.PLoS pathogens · 2020Article
- HIV-1 gp120-CD4-Induced Antibody Complex Elicits CD4 Binding Site-Specific Antibody Response in Mice.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Article
- Structural Vaccinology for Viral Vaccine Design.Frontiers in microbiology · 2019Review
- Glycan Masking Focuses Immune Responses to the HIV-1 CD4-Binding Site and Enhances Elicitation of VRC01-Class Precursor Antibodies.Immunity · 2018Article
- A Universal Approach to Optimize the Folding and Stability of Prefusion-Closed HIV-1 Envelope Trimers.Cell reports · 2018Article
- Brief introduction of current technologies in isolation of broadly neutralizing HIV-1 antibodies.Virus research · 2018Review
- Increased, Durable B-Cell and ADCC Responses Associated with T-Helper Cell Responses to HIV-1 Envelope in Macaques Vaccinated with gp140 Occluded at the CD4 Receptor Binding Site.Journal of virology · 2017Article
- Unique binding modes for the broad neutralizing activity of single-chain variable fragments (scFv) targeting CD4-induced epitopes.Retrovirology · 2017Article
- Induction of a Tier-1-Like Phenotype in Diverse Tier-2 Isolates by Agents That Guide HIV-1 Env to Perturbation-Sensitive, Nonnative States.Journal of virology · 2017Article
29 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
Abstract
The human immunodeficiency virus type 1 (HIV-1) exterior envelope glycoprotein, gp120, possesses conserved binding sites for interaction with the primary virus receptor, CD4, and also for the co-receptor, generally CCR5. Although gp120 is a major target for virus-specific neutralizing antibodies, the gp120 variable elements and its malleable nature contribute to evasion of effective host-neutralizing antibodies. To understand the conformational character and immunogenicity of the gp120 receptor binding sites as potential vaccine targets, we introduced structure-based modifications to stabilize gp120 core proteins (deleted of the gp120 major variable regions) into the conformation recognized by both receptors. Thermodynamic analysis of the re-engineered core with selected ligands revealed significant stabilization of the receptor-binding regions. Stabilization of the co-receptor-binding region was associated with a marked increase in on-rate of ligand binding to this site as determined by surface plasmon resonance. Rabbit immunization studies showed that the conformational stabilization of core proteins, along with increased ligand affinity, was associated with strikingly enhanced humoral immune responses against the co-receptor-binding site. These results demonstrate that structure-based approaches can be exploited to stabilize a conformational site in a large functional protein to enhance immunogenic responses specific for that region.
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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.