Identification and Characterization of the Vibrio vulnificus malPQ Operon

  • LIM MOON SUB (Department of Food Science and Technology, and School of Agricultural Biotechnology, Center for Agricultural Biomaterials, Seoul National University) ;
  • LEE MYUNG HEE (Department of Food Science and Technology, Department of Molecular Biotechnology, Institute of Biotechnology, Chonnam National University) ;
  • LEE JEONG HYUN (Department of Food Science and Technology, Department of Molecular Biotechnology, Institute of Biotechnology, Chonnam National University) ;
  • JU HYUN-MOK (Department of Food Science and Technology, Department of Molecular Biotechnology, Institute of Biotechnology, Chonnam National University) ;
  • PARK NA YOUNG (Department of Food Science and Technology, and School of Agricultural Biotechnology, Center for Agricultural Biomaterials, Seoul National University) ;
  • JEONG HYE SOOK (Department of Food Science and Technology, and School of Agricultural Biotechnology, Center for Agricultural Biomaterials, Seoul National University) ;
  • RHEE JEE EUN (Department of Food Science and Technology, and School of Agricultural Biotechnology, Center for Agricultural Biomaterials, Seoul National University) ;
  • CHOI SANG HO (Department of Food Science and Technology, and School of Agricultural Biotechnology, Center for Agricultural Biomaterials, Seoul National University)
  • 발행 : 2005.06.01

초록

It is likely that maltose could provide a good substrate for the bacteria in the intestine, when the pathogenic bacteria invade and colonize in human gut. For better understanding of this organism's maltose metabolism, a mutant that was not able to grow with maltose as a sole carbon source was screened from a library of mutants constructed by a random transposon mutagenesis. By a transposon-tagging method, malPQ genes encoding a maltodextrin phosphorylase and a 4-${\alpha}$-glucanotransferase, were identified and cloned from Vibrio vulnificus. The deduced amino acid sequences of malPQ from V. vulnificus were 48 to $91\%$ similar to those of MalP and MalQ reported from other Enterobacteriaceae. Functions of malPQ genes were assessed by the construction of mutants whose malPQ genes were inactivated by allelic exchanges. When maltose was used as the sole carbon source, neither malP nor malQ mutant was able to grow to a substantial level, revealing that the MalP and MalQ are the only enzymes for metabolic utilization of maltose. The malQ mutant exhibited decreased adherence toward intestinal epithelial cells in vitro, but there was no difference in the $LD_{50}s$ of the wild-type and the malQ mutant in mice. Therefore, it appears that MalQ is less important in the pathogenesis of V. vulnificus than would have been predicted by considering maltose as a most common sugar in the intestine, but not completely dispensable for virulence in mice.

키워드

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