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.
Wang
H
H
Department of Microbiology, Medical College of Ohio, Toledo 43699-0008, USA.
Lottenberg
R
R
Boyle
M D
MD
D015119:Aminocaproic Acid / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D010958:Plasminogen / Q000378:metabolism*; D010960:Plasminogen Activators / Q000378:metabolism; D011485:Protein Binding; D013297:Streptococcus pyogenes / Q000187:drug effects / Q000378:metabolism* / Q000472:pathogenicity; D013300:Streptokinase / Q000378:metabolism*
D005340:Fibrinogen; D010958:Plasminogen; D013300:Streptokinase; D010960:Plasminogen Activators; D015119:Aminocaproic Acid