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Synthetic glycopeptides reveal the glycan specificity of HIV-neutralizing antibodies

Academic Article
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Overview

authors

  • Amin, M. N.
  • McLellan, J. S.
  • Huang, W.
  • Orwenyo, J.
  • Burton, Dennis
  • Koff, W. C.
  • Kwong, P. D.
  • Wang, L. X.

publication date

  • August 2013

journal

  • Nature Chemical Biology  Journal

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 Manâ‚…GlcNAcâ‚‚ 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.

subject areas

  • AIDS Vaccines
  • Antibodies, Neutralizing
  • Epitopes
  • Glycopeptides
  • HIV-1
  • Polysaccharides
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Identity

PubMed Central ID

  • PMC3730851

International Standard Serial Number (ISSN)

  • 1552-4450

Digital Object Identifier (DOI)

  • 10.1038/nchembio.1288

PubMed ID

  • 23831758
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Additional Document Info

start page

  • 521

end page

  • 526

volume

  • 9

issue

  • 8

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