Complement receptor type 2 (CR2/CD21) is essential for the attachment of Epstein-Barr
virus (EBV) to the surface of B-lymphocytes in an interaction mediated by the viral envelope
glycoprotein gp350. The heavily glycosylated structure of EBV gp350 has recently been
elucidated by x-ray crystallography, and the CR2 binding site on this protein has been
characterized. To identify the corresponding gp350 binding site on CR2, we have
undertaken a site-directed mutagenesis study targeting regions of CR2 that have previously …