AIM: To observe the binding activity of beta-2-glycoprotein I (β2GPI) to hepatitis B surface antigen (HBsAg) and the possible roles of β2GPI in hepatitis B virus (HBV) infection.METHODS: The rationale of ELISA metho...AIM: To observe the binding activity of beta-2-glycoprotein I (β2GPI) to hepatitis B surface antigen (HBsAg) and the possible roles of β2GPI in hepatitis B virus (HBV) infection.METHODS: The rationale of ELISA methods and ELISAbased research method and ligand-blotting technique were used to detect the specific interaction of β2GPI with HBsAg.RESULTS: With the increase of rHBsAg, the binding of β2GPI to rHBsAg elevated, and these changes had statistic significance. When we added non- biotinlyated β2GPI, the OD value significantly decreased though they still were positively relevant to rHBsAg, suggesting non- biotinlyated β2GPI competed with biotinlyated β2GPI 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 β2GPI and BSA,suggesting the affinity of β2GPI to rHBsAg was specific. The ligand blotling indicated that β2GPI might bind to rHBsAg no matter whether it was under reduced condition or not.CONCLUSION: The binding of β2GPI to HBsAg suggests that β2GPI may be a carrier of HBV and that β2GPI may play important roles in HBV infection.展开更多
基金the National Natural Science Foundation of China, No.30070338
文摘AIM: To observe the binding activity of beta-2-glycoprotein I (β2GPI) to hepatitis B surface antigen (HBsAg) and the possible roles of β2GPI in hepatitis B virus (HBV) infection.METHODS: The rationale of ELISA methods and ELISAbased research method and ligand-blotting technique were used to detect the specific interaction of β2GPI with HBsAg.RESULTS: With the increase of rHBsAg, the binding of β2GPI to rHBsAg elevated, and these changes had statistic significance. When we added non- biotinlyated β2GPI, the OD value significantly decreased though they still were positively relevant to rHBsAg, suggesting non- biotinlyated β2GPI competed with biotinlyated β2GPI 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 β2GPI and BSA,suggesting the affinity of β2GPI to rHBsAg was specific. The ligand blotling indicated that β2GPI might bind to rHBsAg no matter whether it was under reduced condition or not.CONCLUSION: The binding of β2GPI to HBsAg suggests that β2GPI may be a carrier of HBV and that β2GPI may play important roles in HBV infection.
