Herpes simplex virus type 1 Fc receptor protects infected cells from antibody-dependent cellular cytotoxicity.
Recent studies indicate that the herpes simplex virus type 1 (HSV-1) Fc receptor (FcR) can bind antiviral immunoglobulin G by participating in antibody bipolar bridging. This occurs when the Fab domain of an immunoglobulin G molecule binds to its antigenic target and the Fc domain binds to the HSV-1 FcR. In experiments comparing cells infected with wild-type HSV-1 (NS) and cells infected with an FcR-deficient mutant (ENS), we demonstrate that participation of the HSV-1 FcR in antibody bipolar bridging reduces the effectiveness of antibody-dependent cellular cytotoxicity.
Dubin
G
G
Department of Medicine, University of Pennsylvania, Philadelphia.
Socolof
E
E
Frank
I
I
Friedman
H M
HM
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000920:Antibody-Dependent Cell Cytotoxicity; D000943:Antigens, Differentiation / Q000235:genetics / Q000276:immunology*; D002460:Cell Line; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology*; D007700:Kinetics; D051379:Mice; D008954:Models, Biological; D011961:Receptors, Fc / Q000235:genetics / Q000276:immunology*; D017452:Receptors, IgG; D018139:Simplexvirus / Q000235:genetics / Q000276:immunology*
D000911:Antibodies, Monoclonal; D000943:Antigens, Differentiation; D007074:Immunoglobulin G; D011961:Receptors, Fc; D017452:Receptors, IgG