Antibody light chain-catalyzed hydrolysis of a hepatitis C virus peptide.
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).
Taguchi
Hiroaki
H
Chemical Immunology and Therapeutics Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, 6431 Fannin, 77030, USA.
Keck
Zhenyong
Z
Foung
Steven K H
SK
Paul
Sudhir
S
Nishiyama
Yasuhiro
Y
D000911:Antibodies, Monoclonal / Q000378:metabolism; D002384:Catalysis; D016174:Hepacivirus / Q000276:immunology / Q000378:metabolism*; D018937:Hepatitis C Antibodies / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D007147:Immunoglobulin Light Chains / Q000378:metabolism*; D010446:Peptide Fragments / Q000276:immunology* / Q000378:metabolism*; D019151:Peptide Library; D011994:Recombinant Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000276:immunology* / Q000378:metabolism
D000911:Antibodies, Monoclonal; D018937:Hepatitis C Antibodies; D007147:Immunoglobulin Light Chains; D010446:Peptide Fragments; D019151:Peptide Library; D011994:Recombinant Proteins; D014764:Viral Proteins