Proteomic comparison of Ralstonia solanacearum strains reveals temperature dependent virulence factors.

作者: Ana M Bocsanczy , Ute CM Achenbach , Arianna Mangravita-Novo , Marjorie Chow , David J Norman

DOI: 10.1186/1471-2164-15-280

关键词:

摘要: Ralstonia solanacearum, the causal agent of bacterial wilt, is a genetically diverse plant pathogen present in tropical and subtropical regions world that infects more than 200 species, including economically important solanaceous crops. Most strains R. solanacearum are only pathogenic at temperatures between 25 to 30°C with can cause disease below 20°C considered threat agriculture temperate areas. Identifying key molecular factors distinguish virulent cold from ones not needed develop effective management tools for this pathogen. We compared protein profiles two low temperature when incubated rhizosphere tomato seedlings 30 18°C using quantitative 2D DIGE gel methods. Spot intensities were quantified compared, differentially expressed proteins sequenced identified by mass spectrometry (MS/MS). Four hundred eighteen (418) spots produced 101 unique proteins. The classified Gene Ontology biological processes categories metabolism, cell processes, stress response, transport, secretion, motility, virulence. Identified virulence included catalase (KatE), exoglucanase A (ChbA), drug efflux pump, twitching motility porin (PilQ). Other components putative type VI secretion system. confirmed differential expression 13 candidate genes real time PCR techniques. Global regulators HrpB HrpG also had dependent PCR. involvement discussed. discovery functional system provides new potential mechanism explore. global HrpB, suggest be partially explained differences regulation all strains.

参考文章(56)
Caitilyn Allen, A.C. Hayward, Philippe Prior, Bacterial wilt disease and the Ralstonia solanacearum species complex Bacterial wilt disease and the Ralstonia solanacearum species complex.. ,(2005)
J. G. Elphinstone, The current bacterial wilt situation: a global overview. Bacterial wilt : the disease and the Ralstonia solanacearum species complex. pp. 9- 28 ,(2005)
Jeffrey G. Thomas, François Baneyx, ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Molecular Microbiology. ,vol. 36, pp. 1360- 1370 ,(2002) , 10.1046/J.1365-2958.2000.01951.X
Yaowei Kang, Huanli Liu, Stéphane Genin, Mark A. Schell, Timothy P. Denny, Ralstonia solanacearum requires type 4 pili to adhere to multiple surfaces and for natural transformation and virulence Molecular Microbiology. ,vol. 46, pp. 427- 437 ,(2002) , 10.1046/J.1365-2958.2002.03187.X
PANAGIOTIS F. SARRIS, NICHOLAS SKANDALIS, MICHAEL KOKKINIDIS, NICKOLAS J. PANOPOULOS, In silico analysis reveals multiple putative type VI secretion systems and effector proteins in Pseudomonas syringae pathovars Molecular Plant Pathology. ,vol. 11, pp. 795- 804 ,(2010) , 10.1111/J.1364-3703.2010.00644.X
M. Fegan, Philippe Prior, None, How complex is the Ralstonia solanacearum species complex Bacterial wilt : the disease and the Ralstonia solanacearum species complex. pp. 449- 461 ,(2005)
Steven Slater, Kathryn L. Houmiel, Minhtien Tran, Timothy A. Mitsky, Nancy B. Taylor, Stephen R. Padgette, Kenneth J. Gruys, Multiple β-Ketothiolases Mediate Poly(β-Hydroxyalkanoate) Copolymer Synthesis in Ralstonia eutropha Journal of Bacteriology. ,vol. 180, pp. 1979- 1987 ,(1998) , 10.1128/JB.180.8.1979-1987.1998
Sarka Beranova-Giorgianni, Proteome analysis by two-dimensional gel electrophoresis and mass spectrometry: strengths and limitations Trends in Analytical Chemistry. ,vol. 22, pp. 273- 281 ,(2003) , 10.1016/S0165-9936(03)00508-9
S. Pukatzki, A. T. Ma, D. Sturtevant, B. Krastins, D. Sarracino, W. C. Nelson, J. F. Heidelberg, J. J. Mekalanos, Identification of a conserved bacterial protein secretion system in Vibrio cholerae using the Dictyostelium host model system Proceedings of the National Academy of Sciences of the United States of America. ,vol. 103, pp. 1528- 1533 ,(2006) , 10.1073/PNAS.0510322103