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Journal of Biomedicine and Biotechnology
Volume 2011, Article ID 530926, 5 pages
http://dx.doi.org/10.1155/2011/530926
Research Article

A Proteome Reference Map of the Causative Agent of Melioidosis Burkholderia pseudomallei

1Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok 10400, Thailand
2National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathumthani 12120, Thailand
3Department of Biochemistry, Faculty of Medical Science, Naresuan University, Phitsanulok 65000, Thailand

Received 15 May 2011; Revised 6 July 2011; Accepted 23 July 2011

Academic Editor: Don Mark Estes

Copyright © 2011 Patompon Wongtrakoongate et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. N. J. White, “Melioidosis,” The Lancet, vol. 361, no. 9370, pp. 1715–1722, 2003. View at Publisher · View at Google Scholar · View at Scopus
  2. M. Wheelis, “First shots fired in biological warfare,” Nature, vol. 395, no. 6699, p. 213, 1998. View at Google Scholar · View at Scopus
  3. W. C. Nierman, D. DeShazer, H. S. Kim et al., “Structural flexibility in the Burkholderia mallei genome,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 39, pp. 14246–14251, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  4. M. T. G. Holden, R. W. Titball, S. J. Peacock et al., “Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 39, pp. 14240–14245, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  5. R. A. Moore, S. Reckseidler-Zenteno, H. Kim et al., “Contribution of gene loss to the pathogenic evolution of Burkholderia pseudomallei and Burkholderia mallei,” Infection and Immunity, vol. 72, no. 7, pp. 4172–4187, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  6. C. Ong, C. H. Ooi, D. Wang et al., “Patterns of large-scale genomic variation in virulent and avirulent Burkholderia species,” Genome Research, vol. 14, no. 11, pp. 2295–2307, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  7. P. Wongtrakoongate, N. Mongkoldhumrongkul, S. Chaijan, S. Kamchonwongpaisan, and S. Tungpradabkul, “Comparative proteomic profiles and the potential markers between Burkholderia pseudomallei and Burkholderia thailandensis,” Molecular and Cellular Probes, vol. 21, no. 2, pp. 81–91, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  8. V. Thongboonkerd, M. Vanaporn, N. Songtawee et al., “Altered proteome in Burkholderia pseudomallei rpoE operon knockout mutant: insights into mechanisms of rpoE operon in stress tolerance, survival, and virulence,” Journal of Proteome Research, vol. 6, no. 4, pp. 1334–1341, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  9. Y. Osiriphun, P. Wongtrakoongate, S. Sanongkiet, P. Suriyaphol, V. Thongboonkerd, and S. Tungpradabkul, “Identification and characterization of RpoS regulon and RpoS-dependent promoters in Burkholderia pseudomallei,” Journal of Proteome Research, vol. 8, no. 6, pp. 3118–3131, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  10. P. Pumirat, P. Saetun, S. Sinchaikul, S. T. Chen, S. Korbsrisate, and V. Thongboonkerd, “Altered secretome of Burkholderia pseudomallei induced by salt stress,” Biochimica et Biophysica Acta, vol. 1794, no. 6, pp. 898–904, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  11. M. Schuster, A. C. Hawkins, C. S. Harwood, and E. P. Greenberg, “The Pseudomonas aeruginosa RpoS regulon and its relationship to quorum sensing,” Molecular Microbiology, vol. 51, no. 4, pp. 973–985, 2004. View at Publisher · View at Google Scholar · View at Scopus
  12. P. Utaisincharoen, N. Tangthawornchaikul, W. Kespichayawattana, P. Chaisuriya, and S. Sirisinha, “Burkholderia pseudomallei interferes with inducible nitric oxide synthase (iNOS) production: a possible mechanism of evading macrophage killing,” Microbiology and Immunology, vol. 45, no. 4, pp. 307–313, 2001. View at Google Scholar · View at Scopus
  13. C. Pesavento, G. Becker, N. Sommerfeldt et al., “Inverse regulatory coordination of motility and curli-mediated adhesion in Escherichia coli,” Genes and Development, vol. 22, no. 17, pp. 2434–2446, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  14. P. Pumirat, J. Cuccui, R. A. Stabler et al., “Global transcriptional profiling of Burkholderia pseudomallei under salt stress reveals differential effects on the Bsa type III secretion system,” BMC Microbiology, vol. 10, article 171, 2010. View at Publisher · View at Google Scholar · View at PubMed
  15. A. Tuanyok, H. S. Kim, W. C. Nierman et al., “Genome-wide expression analysis of iron regulation in Burkholderia pseudomallei and Burkholderia mallei using DNA microarrays,” FEMS Microbiology Letters, vol. 252, no. 2, pp. 327–335, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  16. M. T. Ryzlak and R. Pietruszko, “Heterogeneity of glyceraldehyde-3-phosphate dehydrogenase from human brain,” Biochimica et Biophysica Acta, vol. 954, no. 3, pp. 309–324, 1988. View at Google Scholar · View at Scopus
  17. J. M. Armstrong and D. R. Trentham, “The reactions of D glyceraldehyde 3 phosphate with thiols and the holoenzyme of D glyceraldehyde 3 phosphate dehydrogenase and of inorganic phosphate with the acyl holoenzyme,” Biochemical Journal, vol. 159, no. 3, pp. 513–527, 1976. View at Google Scholar · View at Scopus