Characterization of monoclonal antibody binding site to the polymorphic length of hepatitis B surface antigen synthesized in a cell-free system.
A combination of two modern biological techniques, hybridoma and recombinant DNA, was described to screen and characterize a monoclonal antibody binding site. Three monoclonal antibodies, M27, M9 and M01 recognizing to a specific domain of the hepatitis B virus surface antigen (HBsAg), were determined by their ability to immunoprecipitate the in vitro synthesized HBsAg in a polymorphic length. Results indicated that the M9 and M01 both recognize the S region of surface antigen while the M27 binds to the pre-S2 region of surface antigen.
Lo
S J
SJ
Graduate Institute of Microbiology and Immunology, National Yang-Ming Medical College, Taipei, Taiwan, Republic of China.
Sheu
S Y
SY
Huang
J H
JH
Chang
T H
TH
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D001665:Binding Sites; D002474:Cell-Free System; D006514:Hepatitis B Surface Antigens / Q000276:immunology*; D006515:Hepatitis B virus / Q000235:genetics; D051379:Mice; D008807:Mice, Inbred BALB C; D011233:Precipitin Tests; D011487:Protein Conformation
D000911:Antibodies, Monoclonal; D006514:Hepatitis B Surface Antigens