Tanner J, Weis J, Fearon D, Whang Y, Kieff E
Cell. 1987 Jul 17;50(2):203-13. doi: 10.1016/0092-8674(87)90216-9.
The type 2 complement receptor, CR2, a B lymphocyte surface glycoprotein, is known to be a component of the EBV receptor. We now demonstrate that the major EBV outer membrane glycoprotein, gp350/220, is a highly specific ligand for CR2. EBV or beads coated with purified recombinant gp350/220 adsorb to normal B lymphocytes, cap with CR2, become endocytosed into vesicles, and are released into the cytoplasm. This is the first demonstration of herpesvirus glycoprotein-cell glycoprotein receptor interaction in viral adsorption and penetration. The capping of CR2 in response to virus, gp350/220-coated beads, or anti-CR2 monoclonal antibodies is associated with cocapping of surface immunoglobulin. Interaction between CR2 and surface immunoglobulin may be important in modulating the B cell activation that normally follows EBV infection or exposure to antigen.
2型补体受体CR2是一种B淋巴细胞表面糖蛋白，已知是EB病毒受体的一个组成部分。我们现在证明，EB病毒主要外膜糖蛋白gp350/220是CR2的高度特异性配体。EB病毒或包被纯化重组gp350/220的珠子吸附到正常B淋巴细胞上，与CR2形成帽状结构，被内吞到囊泡中，然后释放到细胞质中。这是疱疹病毒糖蛋白与细胞糖蛋白受体相互作用在病毒吸附和穿透过程中的首次证明。CR2因病毒、包被gp350/220的珠子或抗CR2单克隆抗体而形成帽状结构，这与表面免疫球蛋白的共帽状形成有关。CR2与表面免疫球蛋白之间的相互作用可能在调节EB病毒感染或接触抗原后正常发生的B细胞活化中起重要作用。
