Epstein-Barr virus gp350/220 binding to the B lymphocyte C3d receptor mediates adsorption, capping, and endocytosis.
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.
D000327:Adsorption; D000956:Antigens, Viral / Q000276:immunology / Q000378:metabolism*; D001402:B-Lymphocytes / Q000276:immunology / Q000502:physiology* / Q000648:ultrastructure; D002460:Cell Line; D002478:Cells, Cultured; D004705:Endocytosis; D004854:Herpesvirus 4, Human / Q000502:physiology*; D006801:Humans; D008213:Lymphocyte Activation; D008854:Microscopy, Electron; D011951:Receptors, Complement / Q000378:metabolism*; D017464:Receptors, Complement 3d; D011991:Receptors, Virus / Q000378:metabolism*; D014763:Viral Matrix Proteins
D000956:Antigens, Viral; C037662:EBV-associated membrane antigen, Epstein-Barr virus; D011951:Receptors, Complement; D017464:Receptors, Complement 3d; D011991:Receptors, Virus; D014763:Viral Matrix Proteins