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Fractional Analysis of Escherichia coli O157:H7 by Mass Spectrometry-Based Proteomics
Final rept. Oct 2010-Sep 2011
ARMY EDGEWOOD CHEMICAL BIOLOGICAL CENTER APG MD
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This report is required for the U.S. Army Edgewood Chemical Biological Center In-House Laboratory Independent Research project Membrane Vesicles and Extracellular Proteins in Antibiotic Resistance and Virulence . Certain extracellular proteins of pathogenic bacteria have been shown to function in survival mechanisms such as host immune system modulation Vranakis, et al., July 27, 2011, J. Proteome Res. DOI 10.1021pr200422f and biofilm formation Ostrowski, A., et al., 2011, J. Bacteriol. 1934043. To begin to address this possibility, we have analyzed Escherichia coli O157H7 protein fractions by liquid chromatography-tandem mass spectrometry, followed by biochemical pathway mapping using the Kyoto Encyclopedia of Genes and Genomes. The fimbriae-specific subset included proteins involved in carbohydrate metabolism, which are important in providing energy for fimbriae motion. Moreover, inositol monophosphatase IMP, which has a role in streptomycin synthesis, and a glucose-specific phosphotransferase system G-PTS, involved in environmental processing, were also identified. IMP, G-PTS, and a putative stress protein, recently identified in the suspension, are expected to function as part of the bacterial survival mechanisms. This research should provide fundamental knowledge regarding extracellular proteins produced by Gram-negative bacteria. The identification of molecular level components important for survival could prove useful in arenas such as vaccine and antibiotic development.
APPROVED FOR PUBLIC RELEASE