Fibrinogen binding inhibits the fixation of the third component of human complement on surface of groups A, B, C, and G streptococci.
Effects of fibrinogen binding to M protein-positive and -negative streptococci on fixation of the third component of human complement (C3) were determined. In all test cultures of serological groups A, B, C, and G fixation of C3 was observed in normal human serum as revealed by quantitative fluorescent immunoassay. Fibrinogen binding inhibited the fixation of C3 on streptococci. The degree of inhibition was proportional to the extent of fibrinogen binding. Thus, inhibition of C3 fixation was most pronounced in strongly fibrinogen-positive streptococci of groups A, C, and G and not demonstrable in fibrinogen-negative cultures of groups C and G. Trypsinization of the streptococci destroyed their capacity to bind fibrinogen and consequently the inhibitory effects on C3 fixation. The carboxymethylated alpha and beta chains of fibrinogen moderately inhibited C3 fixation whereas gamma chain had no influence. These studies may indicate that fibrinogen binding structures other than M protein could also be involved in streptococcal pathogenicity.
D001665:Binding Sites; D002462:Cell Membrane / Q000276:immunology / Q000378:metabolism; D003176:Complement C3 / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D009895:Opsonin Proteins / Q000276:immunology; D010587:Phagocytosis; D013291:Streptococcus / Q000276:immunology / Q000378:metabolism*; D013292:Streptococcus agalactiae / Q000276:immunology / Q000378:metabolism; D013297:Streptococcus pyogenes / Q000276:immunology / Q000378:metabolism; D014357:Trypsin / Q000494:pharmacology
D003176:Complement C3; D009895:Opsonin Proteins; D005340:Fibrinogen; D014357:Trypsin