目的 研究乙型肝炎表面抗原(HBsAg)与β2糖蛋白Ⅰ(β2GPⅠ)的结合特性,探讨β2GPⅠ在乙型肝炎病毒(HBV)嗜肝性中的作用。方法 采用Western blot技术,研究还原型与非还原型β2GPⅠ与HBsAg的结合特性。结果 还原型与非还原型β2GPⅠ与HBsAg有相同的亲和力,推测β2GPⅠ与HBsAg的结合部位是在一级结构上相邻的氨基酸残基肽段,与空间构象关系不大。结论 HBV与β2GPⅠ有特异的亲和能力,这一亲和能力可能在HBV感染肝细胞过程中发挥了重要作用,是HBV嗜肝性的原因之一。
Objective To further study the binding character of hepatitis B surface antigen (HBsAg) and beta 2- glycoprotein Ⅰ ( β2GPⅠ ) and to explore whether β2GPⅠ plays an important role in the hepatotropism of hepatitis B virus. Methods Using Western blot technique, we observed the binding character of the HBsAg with reduced and non-reduced β2GPⅠ . Results rHBsAgs with reduced and non-reduced β2GPⅠ showed identical binding activity. Conclusions The binding activity of HBsAg is dependent on tandem residues, but not on conformational structures of β2GPⅠ . There is a specific binding between HBV and β2GPⅠ, which may play an important role in HBV infection and is one of the reasons of hepatotropism of HBV.