New Roles of Glucose-Specific Enzyme IIA of the Vibrio vulnificus Phosphoransferase System

  • Kim, You-Jin (Department of Biological Sciences, and Institute of Microbiology, Seoul National University) ;
  • Koo, Byoung-Mo (Department of Biological Sciences, and Institute of Microbiology, Seoul National University) ;
  • Ryu, Yang-Kyun (Department of Biological Sciences, and Institute of Microbiology, Seoul National University) ;
  • Park, Soon-Jung (Department of Parasitology and Institute of Tropical Medicine, Yonsei University) ;
  • Lee, Kyu-Ho (Department of Environmental Science, Hankuk University of Foreign Studies) ;
  • Seok, Yeong-Jae (Department of Biological Sciences, and Institute of Microbiology, Seoul National University)
  • Published : 2006.05.03

Abstract

In a previous report, we showed that enzyme $IIA^{Glc}(EIIA^{Glc}$ of Escherichia coli phosphotransferase system (PTS) interacts with and regulates activity of FrsA (fermentation/respiration switch protein). A BLAST search revealed that orthologs of FrsA exist only in some Gram-negative bacteria such as E. coli, Salmonella typhimurium, Shigella flexneri, Yersinia pestis, Vibrio cholerae, Vibrio vulnificus, Vibrio parahemeolyticus, and Photorhabdus luminescens and all of these species are facultative anaerobes belonging to the ${\gamma}-proteobacterial$ group, and most of them are highly pathogenic. Ligand-fishing experiments using $EIIA^{Glc}$ of Vibrio vulnificus ($vEIIA^{Glc}$) as bait revealed that $vEIIA^{Glc}$ also interacts with vFrsA in a phosphorylation state-dependent manner. The frsA mutant of Vibrio vulnificus showed remarkably reduced cytotoxicity to HeLa cells and reduced lethality to mice compared to wild type. Comparison of extracellular proteomes between the mutant and wild type indicated that hemolysin was not produced in the frsA mutant. Characterization of another protein interacting with $vEIIA^{Glc}$ will be discussed.

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