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Proteomic approaches to Salmonella Pathogenicity Island 2 encoded proteins and the SsrAB regulon
Author(s) -
Deiwick Jörg,
Rappl Catherine,
Stender Silke,
Jungblut Peter R.,
Hensel Michael
Publication year - 2002
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/1615-9861(200206)2:6<792::aid-prot792>3.0.co;2-v
Subject(s) - pathogenicity island , virulence , biology , salmonella enterica , regulon , salmonella , type three secretion system , secretion , bacterial outer membrane , plasmid , microbiology and biotechnology , recombinant dna , secretory protein , membrane protein , proteomics , gene , bacteria , escherichia coli , genetics , biochemistry , membrane
Type III protein secretion is a common virulence determinant in Gram‐negative bacteria and the genetic information is often clustered in pathogenicity islands or on virulence plasmids. We have analyzed the type III secretion system encoded by Salmonella Pathogenicity Island 2 (SPI2) that is indispensable for systemic disease of Salmonella enterica serotype Typhimurium ( S . Typhimurium) in mice. Since the low abundance of this secretion system restricted direct analysis by proteomic approaches, several putative proteins were expressed as recombinant products and analyzed by two‐dimensional electrophoresis. The map obtained for SPI2 encoded proteins was correlated to the expression pattern of S. Typhimurium. The latter was compared to the proteins induced by SsrAB, the two‐component system regulating SPI2 gene expression. Our results exemplify that recombinant expression is a complementary tool for analysis of low abundant proteins or membrane proteins. This approach contributes to the characterization of these proteins by subcellular fractionation. Furthermore, we show that pulse labeling was necessary to analyze growth phase regulated SPI2 proteins that might not be otherwise detectable.