Epstein-Barr virus gp350/220 binding to the B lymphocyte C3d receptor mediates adsorption, capping, and endocytosis

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adsorption
  • Antigens, Viral / immunology
  • Antigens, Viral / metabolism*
  • B-Lymphocytes / immunology
  • B-Lymphocytes / physiology*
  • B-Lymphocytes / ultrastructure
  • Cell Line
  • Cells, Cultured
  • Endocytosis
  • Herpesvirus 4, Human / physiology*
  • Humans
  • Lymphocyte Activation
  • Microscopy, Electron
  • Receptors, Complement / metabolism*
  • Receptors, Complement 3d
  • Receptors, Virus / metabolism*
  • Viral Matrix Proteins*


  • Antigens, Viral
  • EBV-associated membrane antigen, Epstein-Barr virus
  • Receptors, Complement
  • Receptors, Complement 3d
  • Receptors, Virus
  • Viral Matrix Proteins