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ID 34163
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Author
Miyoshi, Shin-ichi
Watanabe, Hirofumi
Kawase, Tomoka
Shinoda, Sumio
Abstract

Vibrio vulnificus is an opportunistic human pathogen causing septicemia, and the infection is characterized by formation of the edematous skin lesions on limbs. This pathogenic species secretes a thermolysin-like metalloprotease as a virulence determinant. The metalloprotease was confirmed to activate human factor XII-plasma kallikrein-kinin cascade that results in liberation of bradykinin, a chemical mediator enhancing the vascular permeability, from high-molecular weight kininogen. Namely, the metalloprotease showed to generate active fragments by cleavage of Arg-Ile, Arg-Val or Gly-Leu peptide bond in human zymogens (plasma prekallikrein and factor XII). In spite of induction of the sufficient vascular permeability-enhancing and edema-forming reaction in the guinea pig model, a serine protease from V. parahaemolyticus, a human pathogen causing primarily watery diarrhea, showed far less ability to activate and to cleave the human zymogens. These results in part may explain why only V. vulnificus often causes serious edematous skin damages in humans.

Keywords
vibrio vulnificus
vibrio parahaemolyticus
protease
factor XII
plasma prekallikrein
Note
Digital Object Identifer:10.1016/j.toxicon.2004.08.013
Published with permission from the copyright holder. This is the institute's copy, as published in Toxicon, December 2004, Volume 44, Issue 8, Pages 887-893.
Publisher URL:http://dx.doi.org/10.1016/j.toxicon.2004.08.013
Direct access to Thomson Web of Science record
Copyright © 2004 Elsevier Ltd. All rights reserved.
Published Date
2004-12
Publication Title
Toxicon
Volume
volume44
Issue
issue8
Start Page
887
End Page
893
Content Type
Journal Article
language
英語
Refereed
True
DOI
Web of Science KeyUT
Submission Path
pharmacology_general/2