Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Cell Death Mediated by Vibrio parahaemolyticus Type III Secretion System 1 Is Dependent on ERK1/2 MAPK, but Independent of Caspases

  • Yang, Yu-Jin (Department of Environmental Medical Biology and Institute of Tropical Medicine, The Brain Korea 21 Project, Yonsei University College of Medicine) ;
  • Lee, Na-Kyung (Department of Environmental Medical Biology and Institute of Tropical Medicine, The Brain Korea 21 Project, Yonsei University College of Medicine) ;
  • Lee, Na-Yeon (Department of Environmental Medical Biology and Institute of Tropical Medicine, The Brain Korea 21 Project, Yonsei University College of Medicine) ;
  • Lee, Jong-Woong (Department of Environmental Medical Biology and Institute of Tropical Medicine, The Brain Korea 21 Project, Yonsei University College of Medicine) ;
  • Park, Soon-Jung (Department of Environmental Medical Biology and Institute of Tropical Medicine, The Brain Korea 21 Project, Yonsei University College of Medicine)
  • Received : 2011.04.27
  • Accepted : 2011.06.13
  • Published : 2011.09.28
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Abstract

Vibrio parahaemolyticus, which causes gastroenteritis, wound infection, and septicemia, has two sets of type III secretion systems (TTSS), TTSS1 and TTSS2. A TTSS1-deficient vcrD1 mutant of V. parahaemolyticus showed an attenuated cytotoxicity against HEp-2 cells, and a significant reduction in mouse lethality, which were both restored by complementation with the intact vcrD1 gene. V. parahaemolyticus also triggered phosphorylation of mitogen-activated protein kinases (MAPKs) including p38 and ERK1/2 in HEp-2 cells. The ability to activate p38 and ERK1/2 was significantly affected in a TTSS1-deficient vcrD1 mutant. Experiments using MAPK inhibitors showed that p38 and ERK1/2 MAPKs are involved in V. parahaemolyticus-induced death of HEp-2 cells. In addition, caspase-3 and caspase-9 were processed into active forms in V. parahaemolyticus-exposed HEp-2 cells, but activation of caspases was not essential for V. parahaemolyticus-induced death of HEp-2 cells, as shown by both annexin V staining and lactate dehydrogenase release assays. We conclude that secreted protein(s) of TTSS1 play an important role in activation of p38 and ERK1/2 in HEp-2 cells that eventually leads to cell death via a caspase-independent mechanism.

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