Generation and characterization of a humanized antibody with specificity for preS2 surface antigen of hepatitis B virus

Cited 16 time in scopus
Metadata Downloads
Title
Generation and characterization of a humanized antibody with specificity for preS2 surface antigen of hepatitis B virus
Author(s)
Sung Sup Park; Chun Jeih Ryu; P Gripon; C Guguen-Guillouzo; Hyo Jeong Hong
Bibliographic Citation
Hybridoma, vol. 15, no. 6, pp. 435-441
Publication Year
1996
Abstract
For the prevention of hepatitis B virus (HBV) infection, monoclonal antibodies (mAbs) against the surface antigens of HBV would offer several advantages over the current human polyclonal antibody. We have developed a humanized antibody with specificity for the preS2 surface antigen of HBV and evaluated the neutralizing activity of the humanized antibody. The complementarity-determining regions of the heavy and light chains of a murine monoclonal antibody (H8) were grafted onto the variable regions of a highly homologous human anti-Sm antibody, which were then combined with the constant regions of human γ1 and κ, respectively. The affinity of the resulting humanized antibody (Z6B) was about one tenth that of the chimeric antibody. The new version (ZP39) of the humanized antibody, which was constructed by substituting the heavy-chain framework residue at position 94 of the Z6B with original mouse residue, showed almost the same affinity as that of the chimeric antibody. The evaluation of the HBV neutralizing activity of ZP39 using in vitro infection of adult human hepatocyte primary culture by HBV showed that it had a specific activity that was approximately 1000 times higher than commercially available polyclonal hepatitis B immune globulin. We expect that the present humanized antibody will be useful in the prevention of HBV infection.
ISSN
0272-457X
Publisher
Mary Ann Liebert
DOI
http://dx.doi.org/10.1089/hyb.1996.15.435
Type
Article
Appears in Collections:
Aging Convergence Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.