IMMUNOCHEMICAL PROPERTIES AND SPECIFICITY OF MONOCLONAL-ANTIBODIES TOWARDS THE N AND C-TERMINAL REGIONS OF RECOMBINANT NUCLEOCAPSID PROTEINOF HEPATITIS-C VIRUS (HCCAG)

Highly affine murine monoclonal antibodies (MAB) to recombinant nucleo capsid (core) protein of hepatitis C virus (rHCcAg) expressed in E. co li were obtained. The MABs were analyzed by solid-phase enzyme immunoa ssay (EIA), immunodot, immunoblotting, and competitive immunochemical analysis. For estimating the epitope specificity of MAB, several immun oreactive fragments of different length were cloned from the HCcAg reg ion overlapping 160 N-terminal amino acid (a. a.) residues. Use of the se fragments and the competitive EIA demonstrated that MAB recognize 4 non-overlapping epitopes, 2 of which are localized in the 1-80 a. a. and 2 other in the 80-150 a. a. regions. A protocol of EIA for detecti ng HCcAg using MABs to two nonoverlapping HCcAg epitopes has been desi gned. The sensitivity of double-site sandwich is 1 ng/ml for the recom binant protein.