The contrasting IgG-binding interactions of human and herpes simplex virus Fc receptors.
A virally encoded, high-affinity Fc receptor (FcR) is found on herpes simplex virus type 1 (HSV-1) particles and infected cells where its binding of non-immune IgG protects cells from host-mediated lysis. Whilst mutation or aglycosylation of the IgG CH2 domain reduced binding to human FcR, the interaction with HSV-1 FcR was not affected. However, the HSV-1 FcR, unlike human FcR, discriminates between human IgG1 allotypes, being sensitive to changes at positions 214 (CH1) and 356/358 (CH3), away from its proposed binding site at the CH2-CH3 interface. The biological consequences are not known but this is the first evidence of a major functional difference between IgG1 allotypes.
Department of Pathology, University of Cambridge, Cambridge, UK. kla22@mole.bio.cam.ac.uk
K L
KL
Armour
A
A
Atherton
L M
LM
Williamson
M R
MR
Clark
D000920:Antibody-Dependent Cell Cytotoxicity; D001402:B-Lymphocytes / Q000276:immunology; D001665:Binding Sites; D003165:Complement System Proteins / Q000276:immunology; D014644:Genetic Variation; D018259:Herpesvirus 1, Human / Q000276:immunology*; D006801:Humans; D007074:Immunoglobulin G / Q000235:genetics / Q000276:immunology*; D009000:Monocytes / Q000276:immunology; D016296:Mutagenesis; D011961:Receptors, Fc / Q000235:genetics / Q000276:immunology*; D011994:Recombinant Proteins / Q000276:immunology
D007074:Immunoglobulin G; D011961:Receptors, Fc; D011994:Recombinant Proteins; D003165:Complement System Proteins