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.
The contrasting IgG-binding interactions of human and herpes simplex virus Fc receptors
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K. L. Armour, A. Atherton, L. M. Williamson, M. R. Clark; The contrasting IgG-binding interactions of human and herpes simplex virus Fc receptors. Biochem Soc Trans 1 August 2002; 30 (4): 495–500. doi: https://doi.org/10.1042/bst0300495
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