Influence of dipeptides on the interaction of immunoglobulins with bacterial Fc receptors.
Binding of radiolabeled human IgG to bacteria expressing type I, type II, or type III Fc receptors in the presence of glycyl-glycine, glycyl-tyrosine, glycyl-histidine, glycyl-leucine, or glycyl-phenylalanine was studied. No inhibition of labeled human IgG binding to type I or type III Fc receptor positive bacteria was observed by any of the dipeptides. Inhibition of binding of labeled human IgG1, IgG2, and IgG4, but not IgG3, indicated the presence of two distinct Fc receptors associated with the type II Fc receptor-positive group A streptococcal strain.
D004151:Dipeptides / Q000378:metabolism*; D007074:Immunoglobulin G / Q000378:metabolism*; D011961:Receptors, Fc / Q000378:metabolism*; D017452:Receptors, IgG; D013211:Staphylococcus aureus / Q000276:immunology*; D013291:Streptococcus / Q000276:immunology*; D013297:Streptococcus pyogenes / Q000276:immunology*
D004151:Dipeptides; D007074:Immunoglobulin G; D011961:Receptors, Fc; D017452:Receptors, IgG