ArticleThe Journal of biological chemistry2012
A single residue within the V5 region of HIV-1 envelope facilitates viral escape from the broadly neutralizing monoclonal antibody VRC01.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Diverse paths to broadly neutralizing antibody escape among HIV-1 strains.Nature microbiology · 2026Article
- Resistance mutations that distinguish HIV-1 envelopes with discordant VRC01 phenotypes from multi-lineage infections in the HVTN703/HPTN081 trial: implications for cross-resistance.Journal of virology · 2025Article
- HIV-1 envelope facilitates the development of protease inhibitor resistance through acquiring mutations associated with viral entry and immune escape.Frontiers in microbiology · 2024Article
- To prescreen or not to prescreen for broadly neutralizing antibody sensitivity in HIV cure-related trials.Journal of virus eradication · 2023Article
- A neutralizing antibody target in early HIV-1 infection was recapitulated in rhesus macaques immunized with the transmitted/founder envelope sequence.PLoS pathogens · 2022Article
- Broadly neutralizing antibody-derived CAR T cells reduce viral reservoir in individuals infected with HIV-1.The Journal of clinical investigation · 2021Article
- Article
- Development of Protein- and Peptide-Based HIV Entry Inhibitors Targeting gp120 or gp41.Viruses · 2019Review
- Broadly resistant HIV-1 against CD4-binding site neutralizing antibodies.PLoS pathogens · 2019Article
- Prediction of VRC01 neutralization sensitivity by HIV-1 gp160 sequence features.PLoS computational biology · 2019Article
- Characteristics of Envelope Genes in a Chinese Chronically HIV-1 Infected Patient With Broadly Neutralizing Activity.Frontiers in microbiology · 2019Article
- Article
- Diverse pathways of escape from all well-characterized VRC01-class broadly neutralizing HIV-1 antibodies.PLoS pathogens · 2018Article
- PotentJournal of virology · 2017Article
- Further Characterization of the Bifunctional HIV Entry Inhibitor sCD4-FIMolecular therapy. Nucleic acids · 2017Article
- An HIV gp120-CD4 Immunogen Does Not Elicit Autoimmune Antibody Responses in Cynomolgus Macaques.Clinical and vaccine immunology : CVI · 2016Article
- N463 Glycosylation Site on V5 Loop of a Mutant gp120 Regulates the Sensitivity of HIV-1 to Neutralizing Monoclonal Antibodies VRC01/03.Journal of acquired immune deficiency syndromes (1999) · 2015Article
- HIV-1 fitness cost associated with escape from the VRC01 class of CD4 binding site neutralizing antibodies.Journal of virology · 2015Article
- Identification of a neutralizing epitope within antigenic domain 5 of glycoprotein B of human cytomegalovirus.Journal of virology · 2015Article
- Detailed study of the interaction between human herpesvirus 6B glycoprotein complex and its cellular receptor, human CD134.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
VRC01, a broadly neutralizing monoclonal antibody, is capable of neutralizing a diverse array of HIV-1 isolates by mimicking CD4 binding with the envelope glycoprotein gp120. Nonetheless, resistant strains have been identified. Here, we examined two genetically related and two unrelated envelope clones, derived from CRF08_BC-infected patients, with distinct VRC01 neutralization profiles. A total of 22 chimeric envelope clones was generated by interchanging the loop D and/or V5 regions between the original envelopes or by single alanine substitutions within each region. Analysis of pseudoviruses built from these mutant envelopes showed that interchanging the V5 region between the genetically related or unrelated clones completely swapped their VRC01 sensitivity profiles. Mutagenesis analysis revealed that the asparagine residue at position 460 (Asn-460), a potential N-linked glycosylation site in the V5 region, is a key factor for observed resistance in these strains, which is further supported by our structural modeling. Moreover, changes in resistance were found to positively correlate with deviations in VRC01 binding affinity. Overall, our study indicates that Asn-460 in the V5 region is a critical determinant of sensitivity to VRC01 specifically in these viral strains. The long side chain of Asn-460, and potential glycosylation, may create steric hindrance that lowers binding affinity, thereby increasing resistance to VRC01 neutralization.
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