ArticleJournal of virology2003
A novel human antibody against human immunodeficiency virus type 1 gp120 is V1, V2, and V3 loop dependent and helps delimit the epitope of the broadly neutralizing antibody immunoglobulin G1 b12.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 65 citations in OpenAlex.
- A novel monoclonal antibody targeting the hemagglutinin-neuraminidase of peste des petits ruminants virus maintains neutralizing activity by blocking viral adsorption and receptor interaction.Journal of virology · 2026Article
- Identification of a novel monoclonal antibody derived from the lumpy skin disease virus ORF123 that confers cross-binding and cross-neutralizing activity against Capripoxvirus members.Veterinary research · 2026Article
- Affinity for the Interface Underpins Potency of Antibodies Operating In Membrane Environments.Cell reports · 2020Article
- Brief introduction of current technologies in isolation of broadly neutralizing HIV-1 antibodies.Virus research · 2018Review
- Structural Analysis of the Glycosylated Intact HIV-1 gp120-b12 Antibody Complex Using Hydroxyl Radical Protein Footprinting.Biochemistry · 2017Article
- Immunogenic Display of Purified Chemically Cross-Linked HIV-1 Spikes.Journal of virology · 2015Article
- Binding mode characterization of NBD series CD4-mimetic HIV-1 entry inhibitors by X-ray structure and resistance study.Antimicrobial agents and chemotherapy · 2014Article
- Rapid, quantitative mapping of anti-HIV type 1 envelope serum antibody specificities.AIDS research and human retroviruses · 2013Article
- A human antibody to the CD4 binding site of gp120 capable of highly potent but sporadic cross clade neutralization of primary HIV-1.PloS one · 2013Article
- Article
- Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120.Journal of virology · 2012Article
- Article
- Requirements for empirical immunogenicity trials, rather than structure-based design, for developing an effective HIV vaccine.Archives of virology · 2012Review
- Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by a human monoclonal antibody using chemical modification and mass spectrometric analysis.Journal of the American Society for Mass Spectrometry · 2010Article
- Article
- Inhibition of in vivo HIV infection in humanized mice by gene therapy of human hematopoietic stem cells with a lentiviral vector encoding a broadly neutralizing anti-HIV antibody.Journal of virology · 2010Article
- Crystal structure of a 3B3 variant--a broadly neutralizing HIV-1 scFv antibody.Protein science : a publication of the Protein Society · 2009Article
- Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment.Journal of virology · 2009Article
- Glycosylation site-specific analysis of clade C HIV-1 envelope proteins.Journal of proteome research · 2009Article
- Libraries against libraries for combinatorial selection of replicating antigen-antibody pairs.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The V1/V2 and V3 loops are proximal to the CD4 binding site (CD4bs) of human immunodeficiency virus type 1 (HIV-1) gp120 and undergo conformational change upon CD4 receptor engagement by the HIV-1 envelope spike. Nearly all of the reported monoclonal antibodies (MAbs) against the CD4bs exhibit a very limited capacity to neutralize HIV-1. However, one such human MAb, immunoglobulin G1 (IgG1) b12, is uniquely able to neutralize primary isolates across subtypes with considerable potency. The molecular basis for the anti-HIV-1 activity of b12 is not fully understood but is relevant to vaccine design. Here we describe a novel human MAb, 4KG5, whose binding to monomeric gp120 is moderately enhanced by IgG1 b12. In sharp contrast, 4KG5 binding to gp120 is inhibited by soluble CD4 (sCD4) and by all other (n = 14) anti-CD4bs MAbs tested. 4KG5 is unable to recognize gp120 in which either V1, V2, or V3 has been deleted, and MAbs against the V2 or V3 loops inhibit the binding of 4KG5 to gp120. Moreover, 4KG5 is able to inhibit the binding of the CD4-induced MAbs 17b and X5 in the absence of sCD4, whereas 17b and X5 only weakly inhibit the binding of 4KG5 to gp120. Mutagenesis of gp120 provides further evidence of a discontinuous epitope of 4KG5 that is formed by the V1/V2 loop, the V3 loop, and a portion of the bridging sheet (C4). 4KG5 was isolated as a single-chain Fv from a phage display library constructed from the bone marrow of an HIV-1-seropositive subject (FDA2) whose serum neutralizes HIV-1 across subtypes. Despite its source, we observed no significant neutralization with 4KG5 against the autologous (R2) virus and several other strains of HIV-1. The results suggest a model in which antibody access to the CD4bs on the envelope spike of HIV-1 is restricted by the orientation and/or dynamics of the V1/V2 and V3 loops, and b12 avoids these restrictions.
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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.