Studies on specific interaction of beta-2-glycoprotein I with HBsAg.
OBJECTIVE
To observe the binding activity of beta-2-glycoprotein I(beta(2)GPI) to hepatitis B surface antigen (HBsAg) and the possible roles of beta(2)GPI in hepatitis B virus (HBV) infection.


METHODS
The rationale of ELISA methods and ELISA-based research method and ligand-blotting technique were used to detect the specific interaction of beta(2)GPI with HBsAg.


RESULTS
With the increase of rHBsAg, the binding of beta(2)GPI to rHBsAg elevated, and these changes had statistic significance. When we added non- biotinlyated beta(2)GPI, the OD value significantly decreased though they still were positively relevant to rHBsAg, suggesting non- biotinlyated beta(2)GPI competed with biotinlyated beta(2)GPI to saturate the binding sites on rHBsAg. Meanwhile BSA was used as negative control to substitute for rHBsAg coating the plates. The results indicated no interaction between beta(2)GPI and BSA, suggesting the affinity of beta(2)GPI to rHBsAg was specific. The ligand blotling indicated that beta(2)GPI might bind to rHBsAg no matter whether it was under reduced condition or not.


CONCLUSIONS
The binding of beta(2)GPI to HBsAg suggests that beta(2)GPI may be a carrier of HBV and that beta(2)GPI may play important roles in HBV infection.
Gao
Pu-Jun
PJ
Department of Digestion, 1st Hospital affiliated to Jilin University, Changchun 130021, Jilin Province, China. pujun-gao@163.com
Piao
Yun-Feng
YF
Liu
Xiao-Dong
XD
Qu
Li-Ke
LK
Shi
Yang
Y
Wang
Xiao-Cong
XC
Yang
Han-Yi
HY
D001665:Binding Sites; D001667:Binding, Competitive; D001710:Biotin / Q000378:metabolism; D004797:Enzyme-Linked Immunosorbent Assay; D006023:Glycoproteins / Q000378:metabolism*; D006514:Hepatitis B Surface Antigens / Q000378:metabolism*; D006801:Humans; D011994:Recombinant Proteins / Q000378:metabolism; D053482:beta 2-Glycoprotein I
D006023:Glycoproteins; D006514:Hepatitis B Surface Antigens; D011994:Recombinant Proteins; D053482:beta 2-Glycoprotein I; D001710:Biotin