This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Moore, R. A. Articles by Woods, D. E. Search for Related Content PubMed PubMed Citation Articles by Moore, R. A. Articles by Woods, D. E.

 Previous Article  |  Next Article 

Infection and Immunity, July 2004, p. 4172-4187, Vol. 72, No. 7
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.7.4172-4187.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Contribution of Gene Loss to the Pathogenic Evolution of Burkholderia pseudomallei and Burkholderia mallei

Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary Health Sciences Centre, Calgary, Alberta, Canada T2N 4N1,¹ The Institute for Genome Research, Rockville, Maryland 20850,² U.S. Army Medical Research Institute for Infectious Diseases, Fort Detrick, Maryland 21702-5011³

Received 25 February 2004/ Returned for modification 9 March 2004/ Accepted 12 March 2004

Burkholderia pseudomallei is the causative agent of melioidosis. Burkholderia thailandensis is a closely related species that can readily utilize L-arabinose as a sole carbon source, whereas B. pseudomallei cannot. We used Tn5-OT182 mutagenesis to isolate an arabinose-negative mutant of B. thailandensis. Sequence analysis of regions flanking the transposon insertion revealed the presence of an arabinose assimilation operon consisting of nine genes. Analysis of the B. pseudomallei chromosome showed a deletion of the operon from this organism. This deletion was detected in all B. pseudomallei and Burkholderia mallei strains investigated. We cloned the B. thailandensis E264 arabinose assimilation operon and introduced the entire operon into the chromosome of B. pseudomallei 406e via homologous recombination. The resultant strain, B. pseudomallei SZ5028, was able to utilize L-arabinose as a sole carbon source. Strain SZ5028 had a significantly higher 50% lethal dose for Syrian hamsters compared to the parent strain 406e. Microarray analysis revealed that a number of genes in a type III secretion system were down-regulated in strain SZ5028 when cells were grown in L-arabinose, suggesting a regulatory role for L-arabinose or a metabolite of L-arabinose. These results suggest that the ability to metabolize L-arabinose reduces the virulence of B. pseudomallei and that the genes encoding arabinose assimilation may be considered antivirulence genes. The increase in virulence associated with the loss of these genes may have provided a selective advantage for B. pseudomallei as these organisms adapted to survival in animal hosts.

Editor: J. T. Barbieri

This article has been cited by other articles:

• Schell, M. A., Lipscomb, L., DeShazer, D. (2008). Comparative Genomics and an Insect Model Rapidly Identify Novel Virulence Genes of Burkholderia mallei. J. Bacteriol. 190: 2306-2313 [Abstract] [Full Text]  
• Wu, G., Carter, B., Mafura, M., Liebana, E., Woodward, M. J., Anjum, M. F. (2008). Genetic Diversity among Escherichia coli O157:H7 Isolates and Identification of Genes Linked to Human Infections. Infect. Immun. 76: 845-856 [Abstract] [Full Text]  
• Bernier, S. P., Nguyen, D. T., Sokol, P. A. (2008). A LysR-Type Transcriptional Regulator in Burkholderia cenocepacia Influences Colony Morphology and Virulence. Infect. Immun. 76: 38-47 [Abstract] [Full Text]  
• Shalom, G., Shaw, J. G., Thomas, M. S. (2007). In vivo expression technology identifies a type VI secretion system locus in Burkholderia pseudomallei that is induced upon invasion of macrophages. Microbiology 153: 2689-2699 [Abstract] [Full Text]  
• Malott, R. J., Sokol, P. A. (2007). Expression of the bviIR and cepIR Quorum-Sensing Systems of Burkholderia vietnamiensis. J. Bacteriol. 189: 3006-3016 [Abstract] [Full Text]  
• Watanabe, S., Yamada, M., Ohtsu, I., Makino, K. (2007). {alpha}-Ketoglutaric Semialdehyde Dehydrogenase Isozymes Involved in Metabolic Pathways of D-Glucarate, D-Galactarate, and Hydroxy-L-proline: MOLECULAR AND METABOLIC CONVERGENT EVOLUTION. J. Biol. Chem. 282: 6685-6695 [Abstract] [Full Text]  
• Watanabe, S., Shimada, N., Tajima, K., Kodaki, T., Makino, K. (2006). Identification and Characterization of L-Arabonate Dehydratase, L-2-Keto-3-deoxyarabonate Dehydratase, and L-Arabinolactonase Involved in an Alternative Pathway of L-Arabinose Metabolism: NOVEL EVOLUTIONARY INSIGHT INTO SUGAR METABOLISM. J. Biol. Chem. 281: 33521-33536 [Abstract] [Full Text]  
• INGLIS, T. J. J., ROLIM, D. B., DE QUEIROZ SOUSA, A. (2006). MELIOIDOSIS IN THE AMERICAS. Am J Trop Med Hyg 75: 947-954 [Abstract] [Full Text]  
• Tuanyok, A., Tom, M., Dunbar, J., Woods, D. E. (2006). Genome-Wide Expression Analysis of Burkholderia pseudomallei Infection in a Hamster Model of Acute Melioidosis.. Infect. Immun. 74: 5465-5476 [Abstract] [Full Text]  
• Watanabe, S., Kodaki, T., Makino, K. (2006). A Novel {alpha}-Ketoglutaric Semialdehyde Dehydrogenase: EVOLUTIONARY INSIGHT INTO AN ALTERNATIVE PATHWAY OF BACTERIAL L-ARABINOSE METABOLISM. J. Biol. Chem. 281: 28876-28888 [Abstract] [Full Text]  
• Brouns, S. J. J., Walther, J., Snijders, A. P. L., van de Werken, H. J. G., Willemen, H. L. D. M., Worm, P., de Vos, M. G. J., Andersson, A., Lundgren, M., Mazon, H. F. M., van den Heuvel, R. H. H., Nilsson, P., Salmon, L., de Vos, W. M., Wright, P. C., Bernander, R., van der Oost, J. (2006). Identification of the Missing Links in Prokaryotic Pentose Oxidation Pathways: EVIDENCE FOR ENZYME RECRUITMENT. J. Biol. Chem. 281: 27378-27388 [Abstract] [Full Text]  
• McCombie, R. L., Finkelstein, R. A., Woods, D. E. (2006). Multilocus Sequence Typing of Historical Burkholderia pseudomallei Isolates Collected in Southeast Asia from 1964 to 1967 Provides Insight into the Epidemiology of Melioidosis.. J. Clin. Microbiol. 44: 2951-2962 [Abstract] [Full Text]  
• Watanabe, S., Kodak, T., Makino, K. (2006). Cloning, Expression, and Characterization of Bacterial L-Arabinose 1-Dehydrogenase Involved in an Alternative Pathway of L-Arabinose Metabolism. J. Biol. Chem. 281: 2612-2623 [Abstract] [Full Text]  
• Novak, R. T., Glass, M. B., Gee, J. E., Gal, D., Mayo, M. J., Currie, B. J., Wilkins, P. P. (2006). Development and Evaluation of a Real-Time PCR Assay Targeting the Type III Secretion System of Burkholderia pseudomallei. J. Clin. Microbiol. 44: 85-90 [Abstract] [Full Text]  
• Ojaimi, C., Mulay, V., Liveris, D., Iyer, R., Schwartz, I. (2005). Comparative Transcriptional Profiling of Borrelia burgdorferi Clinical Isolates Differing in Capacities for Hematogenous Dissemination. Infect. Immun. 73: 6791-6802 [Abstract] [Full Text]  
• Cheng, A. C., Currie, B. J. (2005). Melioidosis: Epidemiology, Pathophysiology, and Management. Clin. Microbiol. Rev. 18: 383-416 [Abstract] [Full Text]  
• Reckseidler-Zenteno, S. L., DeVinney, R., Woods, D. E. (2005). The Capsular Polysaccharide of Burkholderia pseudomallei Contributes to Survival in Serum by Reducing Complement Factor C3b Deposition. Infect. Immun. 73: 1106-1115 [Abstract] [Full Text]