An exocellular thermolysin-like metalloprotease produced by Vibrio fluvialis: Purification, characterization, and gene cloning

Shin Ichi Miyoshi, Yuka Sonoda, Hiroko Wakiyama, Md Monzur Rahman, Ken Ichi Tomochika, Sumio Shinoda, Shigeo Yamamoto, Kazuo Tobe

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

An exocellular metalloprotease produced by Vibrio fluvialis, an enteropathogenic vibrio, was purified and characterized. The metalloprotease (V. fluvialis protease [VFP]) was found to have very similar characteristics to V. vulnificus protease, including a molecular mass of 45 kDa, sensitivity to chelating agents or competitive inhibitors for thermolysin-like metalloproteases, and the substrate specificity. The structural gene for VFP was also cloned, and its nucleotide sequence was determined. The deduced amino acid sequence confirmed that VFP was a member of the thermolysin family. VFP, like V. vulnificus protease, showed the haemagglutinating, permeability-enhancing and haemorrhagic activities in addition to the proteolytic activity toward oligopeptide, casein or elastin.

Original languageEnglish
Pages (from-to)127-134
Number of pages8
JournalMicrobial Pathogenesis
Volume33
Issue number3
DOIs
Publication statusPublished - Jan 1 2002

Keywords

  • Haemagglutinin
  • Metalloprotease
  • Protease
  • Thermolysin
  • Vibrio fluvialis

ASJC Scopus subject areas

  • Microbiology
  • Infectious Diseases

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