ArticleJournal of acquired immune deficiency syndromes (1999)2015
N463 Glycosylation Site on V5 Loop of a Mutant gp120 Regulates the Sensitivity of HIV-1 to Neutralizing Monoclonal Antibodies VRC01/03.
Article in Journal of acquired immune deficiency syndromes (1999), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Self-reported neurocognitive complaints in the Swiss HIV Cohort Study: a viral genome-wide association study.Brain communications · 2024Article
- Pseudotyped Viruses for Lyssavirus.Advances in experimental medicine and biology · 2023Article
- Lentil lectin derived fromEmerging microbes & infections · 2021Article
- SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mutations of SARS-CoV-2 spike protein: Implications on immune evasion and vaccine-induced immunity.Seminars in immunology · 2021Review
- SARS-CoV-2 escapebioRxiv : the preprint server for biology · 2020Article
- Pre-existing resistance in the latent reservoir can compromise VRC01 therapy during chronic HIV-1 infection.PLoS computational biology · 2020Article
- Article
- HIV-1 pseudoviruses constructed in China regulatory laboratory.Emerging microbes & infections · 2020Review
- Protein and Glycan Mimicry in HIV Vaccine Design.Journal of molecular biology · 2019Review
- Characteristics of Envelope Genes in a Chinese Chronically HIV-1 Infected Patient With Broadly Neutralizing Activity.Frontiers in microbiology · 2019Article
- Key gp120 Glycans Pose Roadblocks to the Rapid Development of VRC01-Class Antibodies in an HIV-1-Infected Chinese Donor.Immunity · 2016Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundHIV-1 gp120/gp41 is heavily modified by n-linked carbohydrates that play important roles either in correct folding or in shielding vulnerable viral protein surfaces from antibody recognition.
methodsIn our previous work, 25 potential N-linked glycosylation sites (PNGS) of a CRF07_BC isolate of HIV-1 were individually mutated, and the resulting effects on infectivity and antibody-mediated neutralization were evaluated. To further understand the functional role of these PNGS, we generated double and multiple mutants from selected individual PNGS mutants. The effects were then evaluated by examining infectivity and sensitivity to antibody-mediated neutralization by neutralizing monoclonal antibodies (nMAbs) and serum antibodies from HIV-1 positive donors.
resultsInfectivity results showed that, among the 12 combined PNGS mutants, only 197M.1 (N197D/N301Q) lost infectivity completely, whereas all others (except for 197M.6) showed reduced viral infectivity. In terms of neutralization sensitivity to known nMAbs, we found that adding N463Q mutation to all the gp120 mutants containing N197D significantly increased neutralization sensitivity to VRC01 and VRC03, suggesting N197 and N463 have a strong synergistic effect in regulating the neutralizing sensitivity of HIV-1 to the anti-CD4bs nMAbs VRC01/VRC03. Structural analysis based on the available structures of gp120 alone and in complex with CD4 and various nMAbs elucidates a molecular rationale for this experimental observation.
conclusionsThe data indicate that N463 plays an important role in regulating the CD4bs MAbs VRC01/VRC03 sensitivity in the genetic background of N197D mutation of gp120, which should provide valuable information for a better understanding of the interplay between HIV-1 and VRC01/03.
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