Role of α2-macroglobulin in phagocytosis of group A and C streptococci

Abstract

Binding of alpha 2-macroglobulin (alpha 2M) to streptococci and its effects on phagocytosis were investigated. Two types of streptococcal binding sites for alpha 2M were observed: Streptococcus pyogenes from human infections interacted only with native alpha 2M whereas S. dysgalactiae from bovine and S. equi from equine infections bound only a complex of alpha 2M with trypsin (alpha 2M-T). Preincubation of S. pyogenes with native alpha 2M substantially enhanced their phagocytosis by human polymorphonuclear neutrophils (PMN) whereas preincubation with alpha 2M-T was without any effect. On the other hand, incubation of S. dysgalactiae and S. equi with alpha 2M-T markedly reduced their phagocytosis by PMN from the respective host species. Native alpha 2M did not affect the phagocytosis of these streptococci. Digestion of the streptococcal binding sites for alpha 2M and alpha 2M-T pronase abolished the enhancement of phagocytosis of S. pyogenes by native alpha 2M as well as the inhibition of phagocytosis of S. dysgalactiae and S. equi by alpha 2M-T. Thus, binding of alpha 2M or its complexes appeared to play a role in streptococcal pathogenicity.