Browse > Article
http://dx.doi.org/10.5352/JLS.2008.18.11.1606

Regulation of an Outer Membrane Protein, OmpW, Expression and Its Biological Function in Salmonell typhimurium  

Yoo, Ah-Young (Division of Biological Sciences, Pusan National University)
Yu, Jong-Earn (Division of Biological Sciences, Pusan National University)
Yang, Ji-Seon (Division of Biological Sciences, Pusan National University)
Kim, Young-Hee (Division of Biological Sciences, Pusan National University)
Bae, Chang-Ho (The Biodesign Institute, Arizona State University)
Oh, Jeong-Il (Division of Biological Sciences, Pusan National University)
Kang, Ho-Young (Division of Biological Sciences, Pusan National University)
Publication Information
Journal of Life Science / v.18, no.11, 2008 , pp. 1606-1611 More about this Journal
Abstract
Outer membrane proteins (OMPs) expressed in the Gram negative bacteria such as Salmonella play multiple functions including material transports, adhesive factors and reception of external signals. This study has been focused on an OmpW protein known as a protein required to form a hydrophobic porin in outer membrane. We have constructed a S. typhimurium CK10 mutant deleting an ompW gene on chromosome. The CK10 strain was more tolerant to SDS than the wild-type strain did. As increase of salt concentration in the culture media, significantly decreased amount of OmpW protein in cells were detected. The maximum OmpW protein was expressed in the absence of salt supplement. However, the growth of CK10 strain was indistinguishable compared to that of the wild-type strain at the variable osmotic conditions. The biological role of differential OmpW expression in response to osmotic conditions remains to be investigated.
Keywords
Salmonella typhimurium; OmpW; outer membrane protein;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Roland, K., R. Curtiss III. and D. Sizemore. 1999. Construction and evaluation of a $ \bigtriangleup$cya $ \bigtriangleup$crp Salmonella typhimurium strain expressing avian pathogenic Escherichia coli O78 LPS as a vaccine to prevent airsacculitis in chickens. Avian Dis. 43, 429-441.   DOI   ScienceOn
2 Gulig, P. A. and R. Curtiss III. 1987. Plasmid-associated virulence of Salmonella typhimurium. Infect. Immun. 55, 2891-2901.
3 Towbin, H., T. Staehelin and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76, 4350-4354.   DOI   ScienceOn
4 Otto, K. and M. Hermansson. 2004. Inactivation of ompX causes increased interactions of type 1 fimbreated Escherichia coli with abiotic surfaces. J. Bacteriol. pp. 226-234.
5 Abigail, A. S. and D. D. Whitt. 2002. Sallmonella Species, pp. 381-397. In Abigail A. Salyers and Dixie D. Whitt (eds.), Bacterial pathogenesis: A molecular approach. American Society for Microbiology, Washington, D.C.
6 Roschenthaler, R., P. Kindler, P. Herrlich and J. Igbokwe. 1970. The action of nitrofurantoin: inhibition of growth of Escherichia coli K 12 and of IPTG-induced beta-galaotosidase synthesis. Zentralbl Bakteriol. 215, 203-211.
7 Nakayama, K., S. M. Kelly and R. Curtiss III. 1988. Construction of an $ASD^+$ expression-cloning vector: stable maintenance and high level expression of cloned genes in a Salmonella vaccine strain. Biotechnol. 6, 693-697.   DOI
8 Gay, P., D. le Coq, M. Steinmetz, T. Berkelman and C. I. Kado. 1985. Positive selection procedure for entrapment of insertion sequence elements in gram-negative bacteria. J. Bacteriol. 164, 918-921.
9 Sambrook, J., E. F. Fritsch and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
10 Parry, C. M., T. T. Hien, G. Dougan, N. J. White and J. J. Farrar. 2002. Typhoid fever. N. Engl. J. Med. 347, 1770-1782.   DOI   ScienceOn
11 Hong, H., D. R. Patel, L. K. Tamm and B. van den Berg. 2006. The outer membrane protein OmpW forms an eight-stranded $\beta$-barrel with a hydrophobic channel. J. Biol. Chem. 281, 7568-7577.   DOI   ScienceOn
12 Sambrook, J. and D. W. Russel. 2001. Molecular Cloning a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
13 Bertani, G. 1951. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J. Bacteriol. 62, 293-300.
14 Pilsl, H., D. Smajs and V. Braun. 1999. Caracterization of colicin S4 and its receptor, OmpW, a minor protein of the Escherichia coli outer membrane. J. Bacteriol. 181, 3578-81.
15 Xu, C., H. Ren, S. Wang and X. Peng. 2004. Proteomic analysis of salt-sensitive outer membrane proteins of Vibrio parahaemolyticus. Res. Microbiol. 155, 835-842.   DOI   ScienceOn
16 Groisman, E. A. and H. Ochman. 1997. How Salmonella became a pathogen. Trends Microbiol. 5, 343-349.   DOI   ScienceOn