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Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120

Academic Article
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Overview

authors

  • Huang, C. C.
  • Venturi, M.
  • Majeed, S.
  • Moore, M. J.
  • Phogat, S.
  • Zhang, M. Y.
  • Dimitrov, D. S.
  • Hendrickson, W. A.
  • Robinson, J.
  • Sodroski, J.
  • Wyatt, Richard
  • Choe, Hyeryun
  • Farzan, Michael
  • Kwong, P. D.

publication date

  • March 2004

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • The conserved surface of the HIV-1 gp120 envelope glycoprotein that binds to the HIV-1 coreceptor is protected from humoral recognition by multiple layers of camouflage. Here we present sequence and genomic analyses for 12 antibodies that pierce these defenses and determine the crystal structures of 5. The data reveal mechanisms and atomic-level details for three unusual immune features: posttranslational mimicry of coreceptor by tyrosine sulfation of antibody, an alternative molecular mechanism controlling such sulfation, and highly selective V(H)-gene usage. When confronted by extraordinary viral defenses, the immune system unveils novel adaptive capabilities, with tyrosine sulfation enhancing the vocabulary of antigen recognition.

subject areas

  • Acquired Immunodeficiency Syndrome
  • Amino Acid Sequence
  • Antibody Formation
  • Antigens, CD4
  • Crystallography, X-Ray
  • Genes, Immunoglobulin
  • HIV Envelope Protein gp120
  • HIV Infections
  • HIV-1
  • Humans
  • Immunoglobulin Fab Fragments
  • Immunoglobulin Heavy Chains
  • Immunoglobulin Joining Region
  • Immunoglobulin Variable Region
  • Molecular Sequence Data
  • Sulfates
  • Tyrosine
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Identity

PubMed Central ID

  • PMC365685

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0308527100

PubMed ID

  • 14981267
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Additional Document Info

start page

  • 2706

end page

  • 2711

volume

  • 101

issue

  • 9

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