Author/Authors :
Aghasadeghi, MR Pasteur Iinstitute of Iran - Dept of Hepatitis and AIDS, - Tehran, تهران, ايران , Sadat, S M Pasteur Iinstitute of Iran - Dept of Hepatitis and AIDS, - Tehran, تهران, ايران , Budkowska, A Institut Pasteur - Unite Hepacivirus - Paris , Khabiri, A R Pasteur Iinstitute of Iran - Dept of Parasitology - Tehran,, تهران, ايران , Amini, S Pasteur Iinstitute of Iran - Dept of Hepatitis and AIDS, - Tehran, تهران, ايران , Bahramali, G Pasteur Iinstitute of Iran - Dept of Hepatitis and AIDS, - Tehran, تهران, ايران , Naddaf, S R Pasteur Iinstitute of Iran - Dept of Parasitology - Tehran,, تهران, ايران , Roohvand, F Pasteur Iinstitute of Iran - Dept of Hepatitis and AIDS - Tehran,, تهران, ايران
Abstract :
Infection with hepatitis C virus (HCV) is a worldwide problem. Among HCV proteins, core antigen (Ag), besides its importance for diagnostic application is a prime candidate for component of a vaccine. Herein, we report results of studies on production of the hydrophilic domain of core Ag (2-122) in native conformation by an arabinose induction system in E.coli and the primary characterization of this recombinant protein for applications in diagnosis, immunization and mAb production. Recombinant core (r-Core) was able to detect anti-core antibodies in HCV positive serum samples in a dilution rate of 1/3200. It was also capable to elicit a potent anti-HCV humoral immune response in BALB/c mice. Finally, we established two stable clones of hybridoma which shown to produce specific and sensitive mAbs against the core protein. HCV core was able to elicit a broad range of antibody specificities depending on the immunogen conformation. Therefore, it may be possible to get new mAbs with higher affinities towards native conformation of core Ag.
Keywords :
Hepatitis C , HCV core protein , Monoclonal antibody , Total core Ag , Iran