The C-terminal domain promotes the hemorrhagic damage caused by Vibrio vulnificus metalloprotease

S. Miyoshi, K. Kawata, K. Tomochika, Sumio Shinoda, S. Yamamoto

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)


Vibrio vulnificus, an opportunistic human pathogen, produces a 45-kDa zinc metalloprotease (V. vulnificus protease; VVP) as an important virulence determinant. VVP injected intradermally into the dorsal skin causes the hemorrhagic damage through specific degradation of type IV collage in the vascular basement membrane. The N-terminal 35-kDa polypeptide (VVP-N), the catalytic domain, also evoked the hemorrhagic skin reaction within minutes. However, the hemorrhagic activity of VVP-N was one-third of that of VVP. Besides, the proteolytic activity of VVP-N toward the reconstituted basement membrane or type IV collagen was found to be about 50% of VVP. VVP-N, like VVP, was quickly inactivated by an equimolar amount of α2-macroglobulin, a broad-spectrum plasma protease inhibitor. These findings indicate that the C-terminal 10-kDa polypeptide, the substrate-binding domain mediating the effective binding to protein substrates, functions to augment the hemorrhagic reaction of VVP.

Original languageEnglish
Pages (from-to)1883-1886
Number of pages4
Issue number12
Publication statusPublished - 2001


  • Functional domain
  • Hemorrhage
  • Protease
  • Vibrio vulnificus

ASJC Scopus subject areas

  • Toxicology


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