Raji cells, a CR2-positive Burkitt lymphoma cell line, incubated in no
rmal human serum, activate C3 and fix C3-derived fragments. The presen
ce of these molecules on the cell surface does not affect subsequent E
pstein-Barr virus (EBV) binding but it prevents superinfection. On the
other hand, EBV superinfection is enhanced if Raji cells were incubat
ed with heat-inactivated serum whose C3 fragments may bind only throug
h receptor-binding sites. These results indicate that the region on ce
ll surface offering the covalent site to C3 fragments would be essenti
al for EBV superinfection. Incubation of Raji cells for 1 min with EBV
results in the phosphorylation of CR2 and of a high-molecular-weight
protein followed by their dephosphorylation, completed already after 2
0 min. This finding ascribes to EBV a prompt action through its recept
or, different from that of other compounds causing a prolonged CR2 pho
sphorylation. Our data suggest that at least two binding sites are req
uired for EBV superinfection of Raji cells or that specific patterns o
f CR2 phosphorylation may modulate Raji superinfection by EBV.