In vitro neutralization of HSV-2: inhibition by binding of normal IgG and purified Fc to virion Fc receptor (FcR).
We designed experiments to assess the effects of binding of the HSV-2 Fc receptor (FcR) to purified rabbit nonimmune IgG and purified Fc. Purified Fc (75 micrograms) or nonimmune IgG (100 micrograms) when bound to HSV-2 did not reduce infectivity but did protect the virions against thermal inactivation at 37 degrees C. However, preincubation of these two reagents with HSV-2 virions significantly protected against neutralization by specific anti-HSV-2, F(ab')2 purified rabbit antiserum. The blockage of neutralization and protection against thermal inactivation afforded by FcR-Fc interaction on HSV-2 virions provide a tenable mechanism to explain viral persistence in an immune host.
D000818:Animals; D001666:Binding Sites, Antibody; D002294:Carcinoma, Squamous Cell; D002460:Cell Line; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000276:immunology; D007141:Immunoglobulin Fc Fragments / Q000276:immunology*; D007128:Immunoglobulin Fragments / Q000276:immunology*; D007074:Immunoglobulin G / Q000276:immunology*; D007822:Laryngeal Neoplasms; D009500:Neutralization Tests; D011817:Rabbits / Q000276:immunology; D011961:Receptors, Fc / Q000276:immunology*; D018139:Simplexvirus / Q000254:growth & development / Q000276:immunology*; D014771:Virion / Q000276:immunology; D014779:Virus Replication
D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007128:Immunoglobulin Fragments; D007074:Immunoglobulin G; D011961:Receptors, Fc