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Epstein Barr virus/complement C3d receptor is an interferon alpha receptor.
Author(s) -
Delcayre A. X.,
Salas F.,
Mathur S.,
Kovats K.,
Lotz M.,
Lernhardt W.
Publication year - 1991
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1991.tb08025.x
Subject(s) - biology , virology , alpha interferon , receptor , complement (music) , alpha (finance) , interferon , genetics , gene , mutant , medicine , construct validity , nursing , complementation , patient satisfaction
Interferon alpha contains a sequence motif similar to the complement receptor type two (CR2/CD21) binding site on complement fragment C3d. Antibodies against a peptide with the CR2 binding sequence on C3d react with a peptide carrying the IFN alpha CR2 binding motif (residues 92–99) and with recombinant IFN alpha. The IFN alpha‐derived peptide, as well as recombinant IFN alpha, inhibits C3bi/C3d interaction with CR2 on the Burkitt lymphoma Raji. The direct interaction of IFN alpha and CR2 is inhibited by polyclonal anti‐IFN alpha, anti‐CR2 and anti‐C3d peptide antibodies as well as by C3bi/C3d, EBV coat protein gp350/220 and IFN but not by IFN gamma. [125I]IFN alpha binding to Raji cells is inhibited by polyclonal anti‐IFN alpha and anti‐CR2 antibodies, by peptides with the CR2 binding motif and partially by C3bi/C3d. Monoclonal anti‐CR2 antibody HB5, but not OKB‐7, blocks IFN alpha binding to Raji cells. CR2 or CR2‐like molecules may therefore be the major IFN alpha receptors on B lymphocytes.