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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

Authors
 Yang, Yu Jin  ;  Na Kyung Lee  ;  Na Yeon Lee  ;  Jong Woong Lee  ;  Soon-Jung Park 
Citation
 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, Vol.21(9) : 903-913, 2011 
Journal Title
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
ISSN
 1017-7825 
Issue Date
2011
MeSH
Animals ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism* ; BacterialSecretionSystems* ; Caspases/metabolism* ; CellDeath ; CellLine ; Enzyme Activation ; Female ; Humans ; Mice ; Mice, Inbred ICR ; Mitogen-Activated Protein Kinase1/metabolism* ; Mitogen-Activated Protein Kinase 3/metabolism* ; VibrioInfections/enzymology* ; VibrioInfections/microbiology ; VibrioInfections/physiopathology* ; Vibrioparahaemolyticus/genetics ; Vibrioparahaemolyticus/metabolism* ; p38 Mitogen-Activated Protein Kinases/metabolism
Keywords
Vibrio parahaemolyticus ; mitogen-activated protein kinases ; caspases
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 mitogenactivated 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. parahaemolyticusinduced 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 caspaseindependent mechanism.
Files in This Item:
T201103285.pdf Download
DOI
10.4014/jmb.1104.04044
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Tropica Medicine (열대의학교실) > 1. Journal Papers
Yonsei Authors
Park, Soon Jung(박순정) ORCID logo https://orcid.org/0000-0002-0423-1944
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/94140
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