ArticleJournal of virology2004
Evolutionary dynamics of the glycan shield of the human immunodeficiency virus envelope during natural infection and implications for exposure of the 2G12 epitope.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed.
- HIV-1 interaction with aniScience · 2024Article
- Review
- The Current Landscape of mRNA Vaccines Against Viruses and Cancer-A Mini Review.Frontiers in immunology · 2022Review
- HIV-1 Envelope Glycosylation and the Signal Peptide.Vaccines · 2021Review
- Impact of Protein Glycosylation on the Design of Viral Vaccines.Advances in biochemical engineering/biotechnology · 2021Review
- Visualization of the HIV-1 Env glycan shield across scales.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Common evolutionary features of the envelope glycoprotein of HIV-1 in patients belonging to a transmission chain.Scientific reports · 2020Article
- Networks of HIV-1 Envelope Glycans Maintain Antibody Epitopes in the Face of Glycan Additions and Deletions.Structure (London, England : 1993) · 2020Article
- Targeting the N332-supersite of the HIV-1 envelope for vaccine design.Expert opinion on therapeutic targets · 2020Review
- Review
- Protein and Glycan Mimicry in HIV Vaccine Design.Journal of molecular biology · 2019Review
- Bacterially expressed HIV-1 gp120 outer-domain fragment immunogens with improved stability and affinity for CD4-binding site neutralizing antibodies.The Journal of biological chemistry · 2018Article
- Glycosylation of the core of the HIV-1 envelope subunit protein gp120 is not required for native trimer formation or viral infectivity.The Journal of biological chemistry · 2017Article
- The Tetrameric Plant Lectin BanLec Neutralizes HIV through Bidentate Binding to Specific Viral Glycans.Structure (London, England : 1993) · 2017Article
- Human Immunodeficiency Virus (HIV) Separation and Enrichment via the Combination of Antiviral Lectin Recognition and a Thermoresponsive Reagent System.Pharmaceutical research · 2016Article
- Influences on the Design and Purification of Soluble, Recombinant Native-Like HIV-1 Envelope Glycoprotein Trimers.Journal of virology · 2015Article
- Article
- Molecular characterization of HIV-1 subtype C gp-120 regions potentially involved in virus adaptive mechanisms.PloS one · 2014Article
- Relaxation of adaptive evolution during the HIV-1 infection owing to reduction of CD4+ T cell counts.PloS one · 2012Article
- Antigenicity and Immunogenicity in HIV-1 Antibody-Based Vaccine Design.Journal of AIDS & clinical research · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Elucidation of the kinetics of exposure of neutralizing epitopes on the envelope of human immunodeficiency virus type 1 (HIV-1) during the course of infection may provide key information about how HIV escapes the immune system or why its envelope is such a poor immunogen to induce broadly efficient neutralizing antibodies. We analyzed the kinetics of exposure of the epitopes corresponding to the broadly neutralizing human monoclonal antibodies immunoglobulin G1b12 (IgG1b12), 2G12, and 2F5 at the quasispecies level during infection. We studied the antigenicity and sequences of 94 full-length envelope clones present during primary infection and at least 4 years later in four HIV-1 clade B-infected patients. No or only minor exposure differences were observed for the 2F5 and IgG1b12 epitopes between the early and late clones. Conversely, the envelope glycoproteins of the HIV-1 quasispecies present during primary infection did not expose the 2G12 neutralizing epitope, unlike those present after several years in three of the four patients. Sequence analysis revealed major differences at potential N-linked glycosylation sites between early and late clones, particularly at positions known to be important for 2G12 binding. Our study, in natural mutants, confirms that the glycosylation sites N295, N332, and N392 are essential for 2G12 binding. This study demonstrates the relationship between the evolving "glycan shield " of HIV and the kinetics of exposure of the 2G12 epitope during the course of natural infection.
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