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Title: Altered proteome in Burkholderia pseudomallei rpoE operon knockout mutant: Insights into mechanisms of rpoE operon in stress tolerance, survival, and virulence
Authors: Visith Thongboonkerd
Muthita Vanaporn
Napat Songtawee
Rattiyaporn Kanlaya
Supachok Sinchaikul
Shui Tein Chen
Anna Easton
Karen Chu
Gregory J. Bancroft
Sunee Korbsrisate
Mahidol University
Academia Sinica Taiwan
National Taiwan University
London School of Hygiene & Tropical Medicine
Faculty of Medicine, Siriraj Hospital, Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Apr-2007
Citation: Journal of Proteome Research. Vol.6, No.4 (2007), 1334-1341
Abstract: We have previously shown that the alternative sigma factor σE (RpoE), encoded by rpoE, is involved in stress tolerance and survival of Burkholderia pseudomallei. However, its molecular and pathogenic mechanisms remain unclear. In the present study, we applied gel-based, differential proteomics to compare the cellular proteome of an rpoE operon knockout mutant (RpoE Mut) to that of wild-type (K96243 WT) B. pseudomallei. Quantitative intensity analysis (n = 5 gels from 5 individual culture flasks in each group) revealed significantly differential expression of 52 proteins, which were subsequently identified by Q-TOF MS/MS. These included oxidative, osmotic, and other stress response proteins; chaperones; transcriptional/translational regulators; metabolic enzymes; proteins involved in cell wall synthesis, fatty synthesis, glycogen synthesis, and storage; exported proteins; secreted proteins; adhesion molecule; protease/peptidase; protease inhibitor; signaling proteins; and other miscellaneous proteins. The down-regulation of several stress response proteins, chaperones, transcriptional/translational regulators, and proteins involved in cell wall synthesis in RpoE Mut provided some new insights into the mechanisms of the rpoE operon for the stress tolerance and survival of B. pseudomallei. In addition, the proteomic data and in vivo study indicated that the rpoE operon is also involved in the virulence of B. pseudomallei. Our findings underscore the usefulness of proteomics for unraveling pathogenic mechanisms of diseases at the molecular level. © 2007 American Chemical Society.
ISSN: 15353893
Appears in Collections:Scopus 2006-2010

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