Differential gene expression and extracellular secretion of the collagenolytic enzymes by the pathogen Vibrio parahaemolyticus.
Differential gene expression and extracellular secretion of the collagenolytic enzymes by the pathogen Vibrio parahaemolyticus.
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DOI：
10.1111/j.1574-6968.2008.01159.x
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发表时间：
2008-06
影响因子：
2.1
通讯作者：
S. Miyoshi;Yuko Nitanda;K. Fujii;K. Kawahara;Tao Li;Yoko Maehara;T. Ramamurthy;Y. Takeda
中科院分区：
文献类型：
--
作者：
S. Miyoshi;Yuko Nitanda;K. Fujii;K. Kawahara;Tao Li;Yoko Maehara;T. Ramamurthy;Y. Takeda
Vibrio parahaemolyticus, a causative agent of wound infections as well as food poisoning, harbors two collagenase genes: vppC and prtV. When cultivated at 26 degrees 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.
