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Identification and characterization of a peptide that specifically binds the human, broadly neutralizing anti-human immunodeficiency virus type 1 antibody b12

Academic Article
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Overview

authors

  • Zwick, Michael
  • Bonnycastle, L. L. C.
  • Menendez, A.
  • Irving, M. B.
  • Barbas III, Carlos
  • Parren, P. W. H. I.
  • Burton, Dennis
  • Scott, J. K.

publication date

  • 2001

journal

  • Journal of Virology  Journal

abstract

  • Human monoclonal antibody (MAb) b12 recognizes a conformational epitope that overlaps the CD-4-binding site of the human immunodeficiency virus type 1 (HIV-1) envelope. MAb b12 neutralizes a broad range of HIV-1 primary isolates and protects against primary virus challenge in animal models. We report here the discovery and characterization of B2.1, a peptide that binds specifically to MAb b12. B2.1 was selected from a phage-displayed peptide library by using immunoglobulin G1 b12 as the selecting agent. The peptide is a homodimer whose activity depends on an intact disulfide bridge joining its polypeptide chains. Competition studies with gp120 indicate that B2.1 occupies the b12 antigen-binding site. The affinity of b12 for B2.1 depends on the form in which the peptide is presented; b12 binds best to the homodimer as a recombinant polypeptide fused to the phage coat. Originally, b12 was isolated from a phage-displayed Fab library constructed from the bone marrow of an HIV-1-infected donor. The B2.1 peptide is highly specific for b12 since it selected only phage bearing b12 Fab from this large and diverse antibody library.

subject areas

  • Antibodies, Monoclonal
  • Antibodies, Viral
  • HIV Infections
  • HIV-1
  • Humans
  • Immunoglobulin G
  • Neutralization Tests
  • Peptides
  • Protein Binding
  • Sensitivity and Specificity
  • Viral Envelope Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.75.14.6692-6699.2001

PubMed ID

  • 11413337
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Additional Document Info

start page

  • 6692

end page

  • 6699

volume

  • 75

issue

  • 14

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