Identification of an epitope in the major envelope protein of Epstein-Barr virus that mediates viral binding to the B lymphocyte EBV receptor (CR2) Article

Nemerow, GR, Houghten, RA, Moore, MD et al. (1989). Identification of an epitope in the major envelope protein of Epstein-Barr virus that mediates viral binding to the B lymphocyte EBV receptor (CR2) . 56(3), 369-377. 10.1016/0092-8674(89)90240-7

cited authors

  • Nemerow, GR; Houghten, RA; Moore, MD; Cooper, NR

authors

abstract

  • The Epstein-Barr virus gp350 220 envelope protein mediates virus attachment to the EBV C3dg receptor (CR2) of human B lymphocytes. Synthetic peptides corresponding to two regions in gp350 220, which have a similar amino acid sequence with the complement C3dg protein, were used to identify a receptor binding epitope. A peptide corresponding to the N terminus of gp350 220, EDPGFFNVE, bound to purified CR2 and to CR2 positive but not CR2 negative B and T lymphoblastoid cell lines. Soluble monomeric gp350 220 peptide blocked CR2 binding to immobilized EBV, while multimeric forms of the N-terminal gp350 220 peptide conjugated to albumin efficiently blocked recombinant gp350 220 and C3dg binding to B cells as well as EBV-induced B cell proliferation and transformation. These studies indicate that the N-terminal region of gp350 220 plays a crucial role in mediating the earliest stages of EBV infection of B cells and provides a molecular basis for the restricted host cell EBV tropism. © 1989.

publication date

  • February 10, 1989

Digital Object Identifier (DOI)

start page

  • 369

end page

  • 377

volume

  • 56

issue

  • 3