Differential gene expression and extracellular secretion of the collagenolytic enzymes by the pathogen Vibrio parahaemolyticus

Shin Ichi Miyoshi, Yuko Nitanda, Kaori Fujii, Kiyomi Kawahara, Tao Li, Yoko Maehara, Thandavarayan Ramamurthy, Yoshifumi Takeda, Sumio Shinoda

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)

Abstract

Vibrio parahaemolyticus, a causative agent of wound infections as well as food poisoning, harbors two collagenase genes: vppC and prtV. When cultivated at 26°C in gelatin broth supplemented with 3.0% NaCl, significant collagenolytic activity was detected in the culture supernatant at the early stationary phase. Native polyacrylamide gel electrophoresis analysis revealed a 90-kDa protein, and N-terminal amino acid sequencing showed that this protein was VppC, generated through truncation of 72 N-terminal amino acid residues. Additionally, significant expression of only vppC was observed by reverse transcriptase PCR. By contrast, a vppC-negative mutant constructed through single crossover homologous recombination secreted a 50-kDa-collagenolytic enzyme; however, this enzyme was a serine protease that was reported previously. These results suggest that VppC is a primary extracellular collagenase produced by V. parahaemolyticus.

Original languageEnglish
Pages (from-to)176-181
Number of pages6
JournalFEMS Microbiology Letters
Volume283
Issue number2
DOIs
Publication statusPublished - Jun 2008

Keywords

  • Collagenase
  • Protease
  • RT-PCR
  • Vibrio parahaemolyticus

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

Fingerprint Dive into the research topics of 'Differential gene expression and extracellular secretion of the collagenolytic enzymes by the pathogen Vibrio parahaemolyticus'. Together they form a unique fingerprint.

Cite this