ArticleVirology2007
Analysis of the neutralization breadth of the anti-V3 antibody F425-B4e8 and re-assessment of its epitope fine specificity by scanning mutagenesis.
Article in Virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Structural determination of the HIV-1 Variable Region 3 epitope of antibody 19b.Journal of virology · 2026Article
- Unraveling clinical outcomes of long-term cART treatment in HIV-1 patients with or without the Brazilian GWGR motif in the V3 loop.Revista do Instituto de Medicina Tropical de Sao Paulo · 2024Article
- Development and Evaluation of an Ebola Virus Glycoprotein Mucin-Like Domain Replacement System as a New Dendritic Cell-Targeting Vaccine Approach against HIV-1.Journal of virology · 2021Article
- Exploring Viral Interference Using Peptides: Molecular Determinants of HIV-1 Inhibition by a Peptide Derived from Human Pegivirus-1 Envelope Protein E2.ChemMedChem · 2021Article
- IgA as a potential candidate for enteric monoclonal antibody therapeutics with improved gastrointestinal stability.Vaccine · 2020Article
- SERINC5 Inhibits HIV-1 Infectivity by Altering the Conformation of gp120 on HIV-1 Particles.Journal of virology · 2020Article
- Computational-guided determination of the functional role of 447-52D long CDRH3.Protein engineering, design & selection : PEDS · 2018Article
- Stabilization of the gp120 V3 loop through hydrophobic interactions reduces the immunodominant V3-directed non-neutralizing response to HIV-1 envelope trimers.The Journal of biological chemistry · 2018Article
- Prediction of HIV-associated neurocognitive disorder (HAND) from three genetic features of envelope gp120 glycoprotein.Retrovirology · 2018Article
- Display of the HIV envelope protein at the yeast cell surface for immunogen development.PloS one · 2018Article
- Design of HIV Coreceptor Derived Peptides That Inhibit Viral Entry at Submicromolar Concentrations.Molecular pharmaceutics · 2017Article
- Article
- A broad range of mutations in HIV-1 neutralizing human monoclonal antibodies specific for V2, V3, and the CD4 binding site.Molecular immunology · 2015Article
- What Do Chaotrope-Based Avidity Assays for Antibodies to HIV-1 Envelope Glycoproteins Measure?Journal of virology · 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
- Antibody to gp41 MPER alters functional properties of HIV-1 Env without complete neutralization.PLoS pathogens · 2014Article
- 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
- HIV-1 variable loop 2 and its importance in HIV-1 infection and vaccine development.Current HIV research · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The identification of cross-neutralizing antibodies to HIV-1 is important for designing antigens aimed at eliciting similar antibodies upon immunization. The monoclonal antibody (mAb) F425-B4e8 had been suggested previously to bind an epitope at the base of V3 and shown to neutralize two primary HIV isolates. Here, we have assessed the neutralization breadth of mAb F425-B4e8 using a 40-member panel of primary HIV-1 and determined the epitope specificity of the mAb. The antibody was able to neutralize 8 clade B viruses (n=16), 1 clade C virus (n=11), and 2 clade D viruses (n=6), thus placing it among the more broadly neutralizing anti-V3 antibodies described so far. Contrary to an initial report, results from our scanning mutagenesis of the V3 region suggest that mAb F425-B4e8 interacts primarily with the crown/tip of V3, notably Ile(309), Arg(315), and Phe(317). Despite the somewhat limited neutralization breadth of mAb F425-B4e8, the results presented here, along with analyses from other cross-neutralizing anti-V3 mAbs, may facilitate the template-based design of antigens that target V3 and permit neutralization of HIV-1 strains in which the V3 region is accessible to antibodies.
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