Vibrio parahaemolyticus is an important food-borne enteropathogen that encounters various adverse conditions in its native environment or during infection. Effects of mild acid treatment on survival under stress conditions, enteropathogenicity, and protein production in this pathogen were investigated. Logarithmically grown cells, at pH 7.5 shifted to pH 5.0 for 30 min, were more resistant to subsequent acid challenge at pH 4.4. A two-phase adaptive procedure (pH 5.8 for 30 min; pH 5.0 for 30 min) was better than a single-phase procedure for enhancing the acid tolerance of this pathogen. The acid-adapted cells were cross-protected against the challenges of low salinity and thermal inactivation. One-dimensional polyacrylamide gel electrophoresis revealed that proteins with molecular masses of 6.4, 9.0, 13.6, 16.3, 18.9, 22.9, 24.4, 28.3, 33.9, 36.9, 41.2, 47.6, 58.1, 65.6, 80.5, 88.2, and 96.9 kDa were induced or significantly enhanced, while proteins of 25.3, 30.1, 30.7, and 91.7 kDa were significantly inhibited. Two-dimensional polyacrylamide gel electrophoresis revealed that 20 species of proteins were induced or significantly enhanced, while 26 species were inhibited. In assays conducted using the suckling mouse model, enteropathogenicity of the acid-adapted cells was significantly enhanced in terms of intestine/body weight ratio and in vivo recovery of infected cells.

Vibrio parahaemolyticus, an important seafood-associated enteropathogen, usually encounters different adverse conditions in its native or food-processing environment, and the stresses resulting from these conditions may affect the survival of this pathogen and thus change its risk with regard to food hygiene. In this study, we investigated the thermotolerance of V. parahaemolyticus under sublethal heat shock and characterized this response by examining the changes in protein profiles and toxin production. Logarithmically grown cells heat shocked at 42 degrees C for 30 min were more resistant to thermal inactivation at 47 degrees C than were unshocked cells. After the 25 degrees C culture was heat shocked, 24 species of proteins were induced, while 13 species were inhibited, as indicated by polyacrylamide gel electrophoresis. DnaJ-, GroEL-, and GroES-like proteins with molecular sizes of 47, 62, and 12 kDa, respectively, were detected by immunoblotting with antibodies raised against the Escherichia coli proteins. During 1 to 8 h of heat shock, GroEL-like protein was produced in substantial amounts and was present in the periplasmic and extracellular fractions, while DnaJ- and GroES-like proteins were present mainly in the total cellular fraction. DnaK-like protein was not detected; nevertheless, the presence of the dnaK-like genetic element was revealed by Southern blotting. Production of thermostable direct hemolysin, the major virulence factor in V. parahaemolyticus, was enhanced in the cells heat shocked at 42 degrees C but not in those heat shocked at 37 degrees C.

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