Characterization of three novel monoclonal antibodies against hepatitis C virus core protein

✍ Scribed by Moradpour, Darius; Wakita, Takaji; Tokushige, Katsutoshi; Carlson, Rolf I.; Krawczynski, Krzysztof; Wands, Jack R.

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 910 KB
• Volume: 48
• Category: Article
• ISSN: 0146-6615
• DOI: 10.1002/(sici)1096-9071(199603)48:3<234::aid-jmv4>3.0.co;2-9

✦ Synopsis

Three novel monoclonal antibodies (MAbs) were established against a recombinant hepatitis C virus (HCV) core protein derived from cloned genotype 1 b HCV cDNA. MAbs C7-50 and C8-59 recognize a conserved linear epitope represented by amino acid residues 21 to 40 of the nucleocapsid protein. MAb C8-48 is directed against a strainspecific conformational epitope located within the first 82 amino acids. A sensitive two-site MAbbased immunoradiometric assay was established using antibodies directed against distinct epitopes on the nucleocapsid protein. Processed 21 kOacore protein wasdetected by immunoblotting in human hepatocellular carcinoma cell lines and primary adult rat hepatocytes transfected with a cytomegalovirus promoter-driven expression construct. lmmunofluorescence microscopy studies revealed a granular and vesicular cytoplasmic staining pattern. MAb C7-50 was used successfullyto detect HCVcore antigen in chronically infected chimpanzee liver tissue. These MAbs represent important reagents for the study of HCV biology and forthe development of immunodiagnostic assays. o 1996 Wiley-Liss, Inc.