Studies on specific interaction of beta-2-glycoprotein I with HBsAg

来源 :World Journal of Gastroenterology | 被引量 : 0次 | 上传用户:onlymiss
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AIM:To observe the binding activity of beta-2-glycoprotein I(β_2GPI) to hepatitis B surface antigen (HBsAg) and thepossible roles of β_2GPI in hepatitis B virus (HBV) infection.METHODS:The rationale of ELISA methods and ELISA-based research method and ligand-blotting technique wereused to detect the specific interaction of β_2GPI with HBsAg.RESULTS:With the increase of rHBsAg,the binding of β_2GPIto rHBsAg elevated,and these changes had statisticsignificance.When we added non-biotinlyated β_2GPI,theOD value significantly decreased though they still werepositively relevant to rHBsAg,suggesting non-biotinlyatedβ_2GPI competed with biotinlyated β_2GPI to saturate thebinding sites on rHBsAg.Meanwhile BSA was used asnegative control to substitute for rHBsAg coating the plates.The results indicated no interaction between β_2GPI and BSA,suggesting the affinity of β_2GPI to rHBsAg was specific.Theligand blotling indicated that β_2GPI might bind to rHBsAg nomatter whether it was under reduced condition or not.CONCLUSION:The binding of β_2GPI to HBsAg suggeststhat β_2GPI may be a carrier of HBV and that β_2GPI may playimportant roles in HBV infection. AIM: To observe the binding activity of beta-2-glycoprotein I (β_2GPI) to hepatitis B surface antigen (HBsAg) and thepossible roles of β_2GPI 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 β_2GPI with HBsAg.RESULTS: With the increase of rHBsAg, the binding of β_2GPIto rHBsAg elevated, and these changes had statisticsignal. Who we added non-biotinlyatedβ_2GPI, theOD value decreased though they still were positive associated to rHBsAg, suggesting non-biotinlyated β_2GPI competed with biotinly β_2GPI to saturate the binding sites on rHBsAg.Meanwhile BSA was used as negative control to substitute for rHBsAg coating the plates. results indicated no interaction between β_2GPI and BSA, suggesting the affinity of β_2GPI to rHBsAg was specific. Theseligand blotling indicated that β_2GPI might bind to rHBsAg nomatter whether it was under reduced condition or not. CONCLUSION: The binding of β_2GPI to HBsAg suggestst β_2GPI may be a carrier of HBV and that β_2GPI may play role roles in HBV infection.
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