ArticleISRN AIDS2012
Conservation, Compensation, and Evolution of N-Linked Glycans in the HIV-1 Group M Subtypes and Circulating Recombinant Forms.
Article in ISRN AIDS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- Cross-Neutralizing CRF01_AE-Infected Plasma from Malaysia Targets CD4-Binding Site of Human Immunodeficiency Virus Type-1 Envelope Glycoprotein.AIDS research and human retroviruses · 2022Article
- Polyclonal antibody responses to HIV Env immunogens resolved using cryoEM.Nature communications · 2021Article
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- HIV-1CViruses · 2020Article
- Article
- Structural Rearrangements Maintain the Glycan Shield of an HIV-1 Envelope Trimer After the Loss of a Glycan.Scientific reports · 2018Article
- Harnessing post-translational modifications for next-generation HIV immunogens.Biochemical Society transactions · 2018Review
- Integrity of Glycosylation Processing of a Glycan-Depleted Trimeric HIV-1 Immunogen Targeting Key B-Cell Lineages.Journal of proteome research · 2018Article
- Molecular Architecture of the Cleavage-Dependent Mannose Patch on a Soluble HIV-1 Envelope Glycoprotein Trimer.Journal of virology · 2017Article
- Article
- Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein.PLoS computational biology · 2016Article
- Glycan-Dependent Neutralizing Antibodies Are Frequently Elicited in Individuals Chronically Infected with HIV-1 Clade B or C.AIDS research and human retroviruses · 2015Article
- Two classes of broadly neutralizing antibodies within a single lineage directed to the high-mannose patch of HIV envelope.Journal of virology · 2015Article
- NICTABA and UDA, two GlcNAc-binding lectins with unique antiviral activity profiles.The Journal of antimicrobial chemotherapy · 2015Article
- The value of HIV protective epitope research for informed vaccine design against diverse viral pathogens.Expert review of vaccines · 2014Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The "glycan shield" exposed on the surface of the HIV-1 gp120 env glycoprotein has been previously proposed as a novel target for anti-HIV treatments. While such targeting of these glycans provides an exciting prospect for HIV treatment, little is known about the conservation and variability of glycosylation patterns within and between the various HIV-1 group M subtypes and circulating recombinant forms. Here, we present evidence of strong strain-specific glycosylation patterns and show that the epitope for the 2G12 neutralising antibody is poorly conserved across HIV-1 group M. The unique glycosylation patterns within the HIV-1 group M subtypes and CRFs appear to explain their varying susceptibility to neutralisation by broadly cross-neutralising (BCN) antibodies. Compensatory glycosylation at linearly distant yet three-dimensionally proximal amino acid positions appears to maintain the integrity of the glycan shield while conveying resistance to neutralisation by BCN antibodies. We find that highly conserved clusters of glycosylated residues do exist on the gp120 trimer surface and suggest that these positions may provide an exciting target for the development of BCN anticarbohydrate therapies.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.