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Cationic poly electrolytes liquoid and leukocyte extract modulate the binding of immuno globulin g to group a streptococcal fc receptors



Cationic poly electrolytes liquoid and leukocyte extract modulate the binding of immuno globulin g to group a streptococcal fc receptors



Acta Pathologica Microbiologica et Immunologica Scandinavica Section B Microbiology 90(2): 161-168



Various polyelectrolytes were investigated for their capacity to inhibit the binding of human IgG to Fc receptors on group A streptococci type M1. Of the cationic substances, protamine and arginine-rich histone inhibited significantly while lysine-rich histone, concanavalin A, lysozyme, polymyxin B, RNase and tuftsin did not. Of the anionic materials, liquid was inhibitory, in contrast to chondroitin sulfate, dextran sulfate, DNA and heparin. Washing experiments showed that the inhibition was caused by binding of the polyelectrolytes to the streptococci. The finding that heated IgG inhibited the binding of histone to the streptococci also indicated a close relation between the binding sites for these compounds. Diffusion-in-gel experiments with alkaline extract of M1 demonstrated that the substances blocking the IgG Fc-receptor were bound to polyglycerophosphate, suggesting that the inhibition of the IgG uptake was due to interaction with lipoteichoic acid. Leukocyte and platelet extracts (human) could modify the binding of IgG, probably by an enzymatic digestion of the receptors. The arginine-rich histone was also capable of inhibiting the binding of IgG to type M15 group A streptococci and to 1 group G strain. The polyelectrolytes had no effect on the binding of IgG to Staphylococcus aureus or of IgA to type 4 group A streptococci.

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