Crystal structure of a cross-reaction complex between an anti-HIV-1 protease antibody and an HIV-2 protease peptide

J Struct Biol. 2005 Mar;149(3):332-7. doi: 10.1016/j.jsb.2004.11.009.

Abstract

The monoclonal antibody 1696, elicited by HIV-1 protease, inhibits the activity of both HIV-1 and HIV-2 proteases with inhibition constants in the low nanomolar range. The antibody cross-reacts with peptides derived from the N-terminal region of both proteases. The crystal structure of the recombinant single-chain Fv fragment of 1696 complexed with an N-terminal peptide from the HIV-2 protease has been determined at 1.88A resolution. Interactions of the peptide with scFv1696 are compared with the previously reported structure of scFv1696 in complex with the corresponding peptide from HIV-1 protease. The origin of cross-reactivity of mAb1696 with HIV proteases is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antibodies, Monoclonal / chemistry*
  • Aspartic Acid Endopeptidases / chemistry*
  • Aspartic Acid Endopeptidases / genetics
  • Aspartic Acid Endopeptidases / immunology
  • Cross Reactions*
  • Crystallography, X-Ray
  • HIV Antibodies / chemistry*
  • HIV Antibodies / immunology
  • HIV Protease / immunology*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / immunology
  • Protein Conformation
  • Sequence Alignment

Substances

  • Antibodies, Monoclonal
  • HIV Antibodies
  • Peptides
  • Aspartic Acid Endopeptidases
  • HIV Protease
  • p16 protease, Human immunodeficiency virus 2