characterizing the escherichia coli o157h7 proteome including protein associations with higher order assemblies描述蛋白质组e大肠杆菌o157h7包括蛋白质对高阶组件.pdfVIP
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characterizing the escherichia coli o157h7 proteome including protein associations with higher order assemblies描述蛋白质组e大肠杆菌o157h7包括蛋白质对高阶组件
Characterizing the Escherichia coli O157:H7 Proteome
Including Protein Associations with Higher Order
Assemblies
1 2 1 1 1
Rembert Pieper *, Quanshun Zhang , David J. Clark , Shih-Ting Huang , Moo-Jin Suh , John C.
1 1 1 1 2
Braisted , Samuel H. Payne , Robert D. Fleischmann , Scott N. Peterson , Saul Tzipori
1J. Craig Venter Institute, Rockville, Maryland, United States of America, 2 Division of Infectious Diseases, Cummings School of Veterinary Medicine, Tufts University, North
Grafton, Massachusetts, United States of America
Abstract
Background: The recent outbreak of severe infections with Shiga toxin (Stx) producing Escherichia coli (STEC) serotype
O104:H4 highlights the need to understand horizontal gene transfer among E. coli strains, identify novel virulence factors
and elucidate their pathogenesis. Quantitative shotgun proteomics can contribute to such objectives, allowing insights into
the part of the genome translated into proteins and the connectivity of biochemical pathways and higher order assemblies
of proteins at the subcellular level.
Methodology/Principal Findings: We examined protein profiles in cell lysate fractions of STEC strain 86-24 (serotype
O157:H7), following growth in cell culture or bacterial isolation from intestines of infected piglets, in the context of
functionally and structurally characterized biochemical pathways of E. coli. Protein solubilization in the presence of Triton X-
100, EDTA and high salt was followed by size exclusion chromatography into the approximate Mr ranges greater than
280 kDa, 280-80 k
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