TY - JOUR
T1 - Differential gene expression and extracellular secretion of the collagenolytic enzymes by the pathogen Vibrio parahaemolyticus
AU - Miyoshi, Shin Ichi
AU - Nitanda, Yuko
AU - Fujii, Kaori
AU - Kawahara, Kiyomi
AU - Li, Tao
AU - Maehara, Yoko
AU - Ramamurthy, Thandavarayan
AU - Takeda, Yoshifumi
AU - Shinoda, Sumio
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2008/6
Y1 - 2008/6
N2 - 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.
AB - 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.
KW - Collagenase
KW - Protease
KW - RT-PCR
KW - Vibrio parahaemolyticus
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U2 - 10.1111/j.1574-6968.2008.01159.x
DO - 10.1111/j.1574-6968.2008.01159.x
M3 - Article
C2 - 18422626
AN - SCOPUS:43549120743
VL - 283
SP - 176
EP - 181
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
SN - 0378-1097
IS - 2
ER -