Brief Reports
Copyright ©The Author(s) 2003. Published by Baishideng Publishing Group Inc. All rights reserved.
World J Gastroenterol. Sep 15, 2003; 9(9): 2114-2116
Published online Sep 15, 2003. doi: 10.3748/wjg.v9.i9.2114
Studies on specific interaction of beta-2-glycoprotein I with HBsAg
Pu-Jun Gao, Yun-Feng Piao, Xiao-Dong Liu, Li-Ke Qu, Yang Shi, Xiao-Cong Wang, Han-Yi Yang
Pu-Jun Gao, Yun-Feng Piao, Yang Shi, Xiao-Cong Wang, Department of Digestion, 1st Hospital affiliated to Jilin University, Changchun 130021, Jilin Province, China
Xiao-Dong Liu, the Key Laboratory of Radiobiology, Ministry of Public Health, Jilin University, Changchun 130021, Jilin Province, China
Li-Ke Qu, Han-Yi Yang, Department of Biochemistry, School of Basic Medicine, Jilin University, Changchun 130021, Jilin Province, China
Author contributions: All authors contributed equally to the work.
Supported by the National Natural Science Foundation of China, No. 30070338
Correspondence to: Pu-Jun Gao, Department of Digestion, 1st Hospital affiliated to Jilin University, Changchun 130021, Jilin Province, China. pujun-gao@163.com
Telephone: +86-431-5612242
Received: November 5, 2002
Revised: November 23, 2002
Accepted: December 12, 2002
Published online: September 15, 2003
Abstract

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 ELISA-based 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.

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