Identification of an epitope in the major envelope protein of Epstein-Barr virus that mediates viral binding to the B lymphocyte EBV receptor (CR2).
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.
Nemerow
G R
GR
Department of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037.
Houghten
R A
RA
Moore
M D
MD
Cooper
N R
NR
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D001402:B-Lymphocytes / Q000502:physiology*; D001665:Binding Sites; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000032:analysis*; D004854:Herpesvirus 4, Human / Q000502:physiology*; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D011485:Protein Binding; D017464:Receptors, Complement 3d; D011991:Receptors, Virus / Q000502:physiology*; D014759:Viral Envelope Proteins / Q000276:immunology / Q000502:physiology*
D000911:Antibodies, Monoclonal; D000939:Epitopes; D017464:Receptors, Complement 3d; D011991:Receptors, Virus; D014759:Viral Envelope Proteins