ANALYSIS OF THE INTERACTION OF GROUP-A STREPTOCOCCI WITH FIBRINOGEN, STREPTOKINASE AND PLASMINOGEN

Group A streptococci demonstrate a number of distinct ways to interact with the human fibrinolytic system to acquire unregulatable cell-surface enzymatic activity. Interactions between bacteria, fibrinogen, streptokinase and plasminogen resulted in acquisition of cell-associated enzymatic activity that can lyse fibrin clots despite the presence of the major physiological plasmin inhibitor, alpha(2)-antiplasmin. Western blot analysis of extracted streptococcal surface proteins suggested that binding of fibrinogen to M or M-related proteins mediated the capture of streptokinase-plasminogen complexes to the bacteria. The enzymatic complex formed by reaction of bacteria with fibrinogen, streptokinase and plasminogen was found to be more stable in human plasma than pre-formed plasmin bound directly to the same bacteria strain.