Premium
Fibrinolytic and procoagulant activities of Y ersinia pestis and S almonella enterica
Author(s) -
Korhonen T. K.
Publication year - 2015
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1111/jth.12932
Subject(s) - proteases , yersinia pestis , salmonella enterica , microbiology and biotechnology , fibrinolysis , salmonella , yersinia , proteolysis , chemistry , protease , biology , biochemistry , enzyme , virulence , bacteria , psychology , genetics , psychiatry , gene
Summary Pla of the plague bacterium Yersinia pestis and PgtE of the enteropathogen Salmonella enterica are surface‐exposed, transmembrane β‐barrel proteases of the omptin family that exhibit a complex array of interactions with the hemostatic systems in vitro , and both proteases are established virulence factors. Pla favors fibrinolysis by direct activation of plasminogen, inactivation of the serpins plasminogen activator inhibitor‐1 and α 2 ‐antiplasmin, inactivation of the thrombin‐activable fibrinolysis inhibitor, and activation of single‐chain urokinase. PgtE is structurally very similar but exhibits partially different functions and differ in expression control. PgtE proteolysis targets control aspects of fibrinolysis, and mimicry of matrix metalloproteinases enhances cell migration that should favor the intracellular spread of the bacterium. Enzymatic activity of both proteases is strongly influenced by the environment‐induced variations in lipopolysaccharide that binds to the β‐barrel. Both proteases cleave the tissue factor pathway inhibitor and thus also express procoagulant activity.