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Pleiotropic effects of a vibrio extracellular protease on the activation of contact system

Jung Eun Park1, Jong Woo Park1, Weontae Lee2

  • 1Department of Biomedical Science, BK21-plus Research Team for Bioactive Control Technology, National Research Center for Dementia, College of Natural Sciences, Chosun University, Gwangju 501-759, Republic of Korea.

Biochemical and Biophysical Research Communications
|July 5, 2014
PubMed

Insights

Vibrio vulnificus protease vEP-45 activates key factors in blood coagulation and the kallikrein/kinin system. This bacterial enzyme cleaves clotting factors and prekallikrein, impacting hemostasis and vascular permeability.

Area of Science:

  • Microbiology
  • Biochemistry
  • Hematology

Background:

  • Pathogenic bacteria secrete proteases that can disrupt the hemostatic system.
  • Extracellular zinc metalloprotease (vEP-45) from Vibrio vulnificus activates prothrombin to thrombin, forming fibrin clots.

Purpose of the Study:

  • To investigate the effects of vEP-45 on the intrinsic pathway of coagulation.
  • To examine the impact of vEP-45 on the kallikrein/kinin system.

Main Methods:

  • In vitro and plasma milieu assays to assess protease activity.
  • In vivo studies to evaluate vascular permeability induction.

Main Results:

  • vEP-45 proteolytically activated clotting factors FXII, FXI, FX, and prothrombin.
  • Cleavage of plasma prekallikrein (PPK) to kallikrein and digestion of high-molecular weight kininogen (HK) were observed.
  • vEP-45 induced dose-dependent vascular permeability in vivo.

Conclusions:

  • vEP-45 activates the plasma contact system by cleaving key zymogen molecules.
  • The protease participates in both the intrinsic pathway of coagulation and the kallikrein/kinin system.
  • vEP-45 significantly impacts hemostasis and vascular function.
Keywords:
CoagulationContact systemKallikrein/kininVascular permeabilityVibrio vulnificusvEP-45 protease

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