ArticleNature chemical biology2013
Synthetic glycopeptides reveal the glycan specificity of HIV-neutralizing antibodies.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
What it found
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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
72 citing papers in PubMed, 111 citations in OpenAlex.
- O-glycosylation in viruses: A sweet tango.mLife · 2024Review
- An HIV-1 broadly neutralizing antibody overcomes structural and dynamic variation through highly focused epitope targeting.Npj viruses · 2023Article
- Glycoconjugates: Synthesis, Functional Studies, and Therapeutic Developments.Chemical reviews · 2022Review
- Biocatalyzed Synthesis of Glycostructures with Anti-infective Activity.Accounts of chemical research · 2022Review
- Synthesis and Immunological Study of N-Glycan-Bacteriophage Qβ Conjugates Reveal Dominant Antibody Responses to the Conserved Chitobiose Core.Bioconjugate chemistry · 2022Article
- Recent advances on smart glycoconjugate vaccines in infections and cancer.The FEBS journal · 2022Review
- Integrated Chemoenzymatic Approach to Streamline the Assembly of Complex Glycopeptides in the Liquid Phase.Journal of the American Chemical Society · 2022Article
- Chemoenzymatic Synthesis and Antibody Binding of HIV-1 V1/V2 Glycopeptide-Bacteriophage QInternational journal of molecular sciences · 2021Article
- Immunogenicity Evaluation of N-Glycans Recognized by HIV Broadly Neutralizing Antibodies.ACS chemical biology · 2021Article
- Engineering well-expressed, V2-immunofocusing HIV-1 envelope glycoprotein membrane trimers for use in heterologous prime-boost vaccine regimens.PLoS pathogens · 2021Article
- Glycosylation States on Intact Proteins Determined by NMR Spectroscopy.Molecules (Basel, Switzerland) · 2021Article
- Comparative studies on the substrate specificity and defucosylation activity of three α-l-fucosidases using synthetic fucosylated glycopeptides and glycoproteins as substrates.Bioorganic & medicinal chemistry · 2021Article
- Recent Advances in the Chemical Biology ofMolecules (Basel, Switzerland) · 2021Review
- Chemoenzymatic Synthesis of HIV-1 Glycopeptide Antigens.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Cell-Free Synthetic Glycobiology: Designing and Engineering Glycomolecules Outside of Living Cells.Frontiers in chemistry · 2020Review
- Protein and Glycan Mimicry in HIV Vaccine Design.Journal of molecular biology · 2019Review
- Glycopeptides and -Mimetics to Detect, Monitor and Inhibit Bacterial and Viral Infections: Recent Advances and Perspectives.Molecules (Basel, Switzerland) · 2019Review
- Oligomannose Glycopeptide Conjugates Elicit Antibodies Targeting the Glycan Core Rather than Its Extremities.ACS central science · 2019Article
- Chemoenzymatic synthesis of glycopeptides bearing rare N-glycan sequences with or without bisecting GlcNAc.Chemical science · 2018Article
- Chemoenzymatic Methods for the Synthesis of Glycoproteins.Chemical reviews · 2018Review
12 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
A new class of glycan-reactive HIV-neutralizing antibodies, including PG9 and PG16, has been recently discovered that seem to recognize previously uncharacterized glycopeptide epitopes on HIV-1 gp120. However, further characterization and reconstitution of the precise neutralizing epitopes are complicated by the heterogeneity of glycosylation. We report here the design, synthesis and antigenic evaluation of new cyclic V1V2 glycopeptides carrying defined N-linked glycans at the conserved glycosylation sites (Asn160 and Asn156 or Asn173) derived from gp120 of two HIV-1 isolates. Antibody binding studies confirmed the necessity of a Man₅GlcNAc₂ glycan at Asn160 for recognition by PG9 and PG16 and further revealed a critical role of a sialylated N-glycan at the secondary site (Asn156 or Asn173) in the context of glycopeptides for antibody binding. In addition to defining the glycan specificities of PG9 and PG16, the identified synthetic glycopeptides provide a valuable template for HIV-1 vaccine design.
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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.