TY - JOUR
T1 - Fibronectin and asialoglyprotein receptor mediate hepatitis B surface antigen binding to the cell surface
AU - Yang, Jing
AU - Wang, Feng
AU - Tian, Linlin
AU - Su, Jing
AU - Zhu, Xiangqian
AU - Lin, Li
AU - Ding, Xiaoran
AU - Wang, Xuejun
AU - Wang, Shengqi
N1 - Funding Information:
This work was supported by three grants from the National Natural Science Foundation of China (nos. 30530650, 30600531, and 30625041) and special funding from the Major State Basic Research Program of China (973 program) (no. 2005CB522902). We are grateful to Caibing Cui for providing plasmids expressing FN fragments and to many colleagues for helpful discussion during the course of this work.
PY - 2010
Y1 - 2010
N2 - Both fibronectin and the asialoglycoprotein receptor (ASGPR) have been identified by some investigators as partners for hepatitis B virus (HBV) envelope proteins. Because fibronectin is a natural ligand for ASGPR, we speculated that HBV might attach to ASGPR expressed on the hepatocyte surface via fibronectin. To test this hypothesis, we first confirmed by co-immunoprecipitation that ASGPR, fibronectin and HBsAg bind to each other in HepG2.2.15 cells, and possible binding domains were identified by GST pull-down. In addition, by measuring binding of HBsAg to cells, we found that ASGPR and fibronectin enhanced the binding capability of HBsAg to HepG2 cells, and even to 293T and CHO cells, which normally do not bind HBV. In conclusion, our findings suggest that both fibronectin and ASGPR mediate HBsAg binding to the cell surface, which provides further evidence for the potential roles of these two proteins in mediating HBV binding to liver cells.
AB - Both fibronectin and the asialoglycoprotein receptor (ASGPR) have been identified by some investigators as partners for hepatitis B virus (HBV) envelope proteins. Because fibronectin is a natural ligand for ASGPR, we speculated that HBV might attach to ASGPR expressed on the hepatocyte surface via fibronectin. To test this hypothesis, we first confirmed by co-immunoprecipitation that ASGPR, fibronectin and HBsAg bind to each other in HepG2.2.15 cells, and possible binding domains were identified by GST pull-down. In addition, by measuring binding of HBsAg to cells, we found that ASGPR and fibronectin enhanced the binding capability of HBsAg to HepG2 cells, and even to 293T and CHO cells, which normally do not bind HBV. In conclusion, our findings suggest that both fibronectin and ASGPR mediate HBsAg binding to the cell surface, which provides further evidence for the potential roles of these two proteins in mediating HBV binding to liver cells.
UR - http://www.scopus.com/inward/record.url?scp=77953323074&partnerID=8YFLogxK
U2 - 10.1007/s00705-010-0657-5
DO - 10.1007/s00705-010-0657-5
M3 - Article
C2 - 20364278
AN - SCOPUS:77953323074
SN - 0304-8608
VL - 155
SP - 881
EP - 888
JO - Archives of Virology
JF - Archives of Virology
IS - 6
ER -