B형 간염바이러스 S 표면항원에 대한 사람 단일클론 항체의 생산 및 특성연구 = Production and Characterization of Human Monoclonal Antibody to Hepatitis B Surface Antigen

다국어 초록 (Multilingual Abstract)

For the prevention of hepatitis B virus infection, we have constructed a human hybridoma (23HN) secreting a monoclonal antibody (mAb) with specificity for the common 'a' determinant of hepatitis B surface antigen (HBsAg). HBsAg-primed human B lymphocytes were prepared by panning and subsequently activated by Epstein-Barr virus transformation.
The transformed B cells were fused with human-mouse heterohybridoma cells as a fusion partner, and the resulting hybridoma cell clones were isolated and examined for the antibody production. One hybridoma clone 23HN produced the human mAb for 4 months. The heavy and light chains of the mAb were shown to have yl and ic isotypes, respectively. For the characterization of 23HN, the antibody was purified, and its size and purity was confirmed by 10% SDS-PAGE and Western analysis. The epitope analysis showed that 23HN binds to both adr and ay subtypes of hepatitis B virus surface antigen linked by disulfide bridges, suggesting that it re-cognizes a common 'a' antigenic determinant. Competition binding assay using three murine mAbs H67, F39.20 and F5.28.6, which bind to the common 'a' antigenic determinant but their fine epitopes are different from each other, showed that 23HN competes effectively with F39.20, suggesting that the fine epitope of 23HN is same as that of F39.20.
The antigen binding affinity of 23HN was 6 10' M-1. From these results, we expect that the 23HN human mAb may be useful in the prevention or therapy of HBV infection.