ArticleJournal of molecular biology2008
Structure of antibody F425-B4e8 in complex with a V3 peptide reveals a new binding mode for HIV-1 neutralization.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed.
- Structural determination of the HIV-1 Variable Region 3 epitope of antibody 19b.Journal of virology · 2026Article
- Regulation of epitope exposure in the gp41 membrane-proximal external region through interactions at the apex of HIV-1 Env.PLoS pathogens · 2022Article
- Distinct conformations of the HIV-1 V3 loop crown are targetable for broad neutralization.Nature communications · 2021Article
- SERINC5 Inhibits HIV-1 Infectivity by Altering the Conformation of gp120 on HIV-1 Particles.Journal of virology · 2020Article
- Difficult-to-neutralize global HIV-1 isolates are neutralized by antibodies targeting open envelope conformations.Nature communications · 2019Article
- Structural Comparison of Human Anti-HIV-1 gp120 V3 Monoclonal Antibodies of the Same Gene Usage Induced by Vaccination and Chronic Infection.Journal of virology · 2018Article
- Increased Epitope Complexity Correlated with Antibody Affinity Maturation and a Novel Binding Mode Revealed by Structures of Rabbit Antibodies against the Third Variable Loop (V3) of HIV-1 gp120.Journal of virology · 2018Article
- Display of the HIV envelope protein at the yeast cell surface for immunogen development.PloS one · 2018Article
- Current Advances in Virus-Like Particles as a Vaccination Approach against HIV Infection.Vaccines · 2016Review
- Functional and Structural Characterization of Human V3-Specific Monoclonal Antibody 2424 with Neutralizing Activity against HIV-1 JRFL.Journal of virology · 2015Article
- What Do Chaotrope-Based Avidity Assays for Antibodies to HIV-1 Envelope Glycoproteins Measure?Journal of virology · 2015Article
- Identification of CD4-Binding Site Dependent Plasma Neutralizing Antibodies in an HIV-1 Infected Indian Individual.PloS one · 2015Article
- A High Throughput Protein Microarray Approach to Classify HIV Monoclonal Antibodies and Variant Antigens.PloS one · 2015Article
- Structural basis of clade-specific HIV-1 neutralization by humanized anti-V3 monoclonal antibody KD-247.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Article
- Differential glycosylation of envelope gp120 is associated with differential recognition of HIV-1 by virus-specific antibodies and cell infection.AIDS research and therapy · 2014Article
- Computational prediction of neutralization epitopes targeted by human anti-V3 HIV monoclonal antibodies.PloS one · 2014Article
- Rabbit anti-HIV-1 monoclonal antibodies raised by immunization can mimic the antigen-binding modes of antibodies derived from HIV-1-infected humans.Journal of virology · 2013Article
- Characterization of humoral responses to soluble trimeric HIV gp140 from a clade A Ugandan field isolate.Journal of translational medicine · 2013Article
- Max Bergmann lecture protein epitope mimetics in the age of structural vaccinology.Journal of peptide science : an official publication of the European Peptide Society · 2013Review
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Authors and funding
7 authors.
Funding
Abstract
F425-B4e8 (B4e8) is a monoclonal antibody isolated from a human immunodeficiency virus type 1 (HIV-1)-infected individual that recognizes the V3 variable loop on the gp120 subunit of the viral envelope spike. B4e8 neutralizes a subset of HIV-1 primary isolates from subtypes B, C and D, which places this antibody among the very few human anti-V3 antibodies with notable cross-neutralizing activity. Here, the crystal structure of the B4e8 Fab' fragment in complex with a 24-mer V3 peptide (RP142) at 2.8 A resolution is described. The complex structure reveals that the antibody recognizes a novel V3 loop conformation, featuring a five-residue alpha-turn around the conserved GPGRA apex of the beta-hairpin loop. In agreement with previous mutagenesis analyses, the Fab' interacts primarily with V3 through side-chain contacts with just two residues, Ile(P309) and Arg(P315), while the remaining contacts are to the main chain. The structure helps explain how B4e8 can tolerate a certain degree of sequence variation within V3 and, hence, is able to neutralize an appreciable number of different HIV-1 isolates.
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