Antibody light chain-catalyzed hydrolysis of a hepatitis C virus peptide

Bioorg Med Chem Lett. 2004 Sep 6;14(17):4529-32. doi: 10.1016/j.bmcl.2004.06.044.

Abstract

A panel of human monoclonal and recombinant antibody light chains was screened for cleavage of the synthetic peptide corresponding to a neutralizing epitope of hepatitis C virus (residues 192-205 of envelope glycoprotein E1). One of the 39 light chains studied hydrolyzed the Val197-Ser198 bond of the peptide with Km and kcat values of 223 +/- 7 microM and 0.087 +/- 0.001 min(-1).

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies, Monoclonal / metabolism
  • Catalysis
  • Hepacivirus / immunology
  • Hepacivirus / metabolism*
  • Hepatitis C Antibodies / metabolism*
  • Humans
  • Hydrolysis
  • Immunoglobulin Light Chains / metabolism*
  • Peptide Fragments / immunology*
  • Peptide Fragments / metabolism*
  • Peptide Library
  • Recombinant Proteins / metabolism
  • Viral Proteins / immunology*
  • Viral Proteins / metabolism

Substances

  • Antibodies, Monoclonal
  • Hepatitis C Antibodies
  • Immunoglobulin Light Chains
  • Peptide Fragments
  • Peptide Library
  • Recombinant Proteins
  • Viral Proteins