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BioMed Research International
Volume 2015, Article ID 636249, 9 pages
http://dx.doi.org/10.1155/2015/636249
Research Article

Enhanced and Secretory Expression of Human Granulocyte Colony Stimulating Factor by Bacillus subtilis SCK6

1School of Biological Sciences, University of the Punjab, Lahore 54590, Pakistan
2Institute of Biochemistry and Biotechnology, University of the Punjab, Lahore 54590, Pakistan

Received 2 October 2015; Revised 8 December 2015; Accepted 8 December 2015

Academic Editor: Jorge F. B. Pereira

Copyright © 2015 Shaista Bashir 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. S. Sadaf, M. A. Khan, D. B. Wilson, and M. W. Akhtar, “Molecular cloning, characterization, and expression studies of water buffalo (Bubalus bubalis) somatotropin,” Biochemistry, vol. 72, no. 2, pp. 162–169, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. L. Westers, H. Westers, and W. J. Quax, “Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism,” Biochimica et Biophysica Acta—Molecular Cell Research, vol. 1694, no. 1–3, pp. 299–310, 2004. View at Publisher · View at Google Scholar · View at Scopus
  3. Q. M. Chen, Y. Q. Geng, J. Ni, G. F. Wang, and R. Z. Jiang, “Study on Bacillus pumilus as a recipient strain for genetic engineering of Bacillus,” Acta Genetica Sinica, vol. 16, no. 3, pp. 206–212, 1989. View at Google Scholar · View at Scopus
  4. S. Sadaf, H. Arshad, and M. W. Akhtar, “A non-ionic surfactant reduces the induction time and enhances expression levels of bubaline somatotropin in Pichia pastoris,” Molecular Biology Reports, vol. 41, no. 2, pp. 855–863, 2014. View at Publisher · View at Google Scholar · View at Scopus
  5. L. Bredmose, S. Madsen, A. Vrang et al., “Development of a heterologous gene expression system for use in Lactococcus lactis,” in Recombinant Protein Production with Prokaryotic and Eukaryotic Cells. A Comparative View on Host Physiology, pp. 269–275, Springer, 2001. View at Publisher · View at Google Scholar
  6. D. Petsch and F. B. Anspach, “Endotoxin removal from protein solutions,” Journal of Biotechnology, vol. 76, no. 2-3, pp. 97–119, 2000. View at Publisher · View at Google Scholar · View at Scopus
  7. R. V. Datar, T. Cartwright, and C. G. Rosen, “Process economics of animal cell and bacterial fermentations: a case study analysis of tissue plasminogen activator,” Nature Biotechnology, vol. 11, no. 3, pp. 349–357, 1993. View at Publisher · View at Google Scholar
  8. F. G. Durrani, R. Gul, S. Sadaf, and M. W. Akhtar, “Expression and rapid purification of recombinant biologically active ovine growth hormone with DsbA targeting to Escherichia coli inner membrane,” Applied Microbiology and Biotechnology, vol. 99, no. 16, pp. 6791–6801, 2015. View at Publisher · View at Google Scholar
  9. W. Li, X. Zhou, and P. Lu, “Bottlenecks in the expression and secretion of heterologous proteins in Bacillus subtilis,” Research in Microbiology, vol. 155, no. 8, pp. 605–610, 2004. View at Google Scholar
  10. M. Simonen and I. Palva, “Protein secretion in Bacillus species,” Microbiological Reviews, vol. 57, no. 1, pp. 109–137, 1993. View at Google Scholar · View at Scopus
  11. T. Moks, L. Abrahmsén, E. Holmgren et al., “Expression of human insulin-like growth factor I in bacteria: use of optimized gene fusion vectors to facilitate protein purification,” Biochemistry, vol. 26, no. 17, pp. 5239–5244, 1987. View at Publisher · View at Google Scholar · View at Scopus
  12. L. L. Fu, Z. R. Xu, W. F. Li, J. B. Shuai, P. Lu, and C. X. Hu, “Protein secretion pathways in Bacillus subtilis: implication for optimization of heterologous protein secretion,” Biotechnology Advances, vol. 25, no. 1, pp. 1–12, 2007. View at Publisher · View at Google Scholar · View at Scopus
  13. K. H. M. V. Wely, The general protein secretion pathway of Bacillus subtilis [Ph.D. thesis], University of Groningen, Groningen, The Netherlands, 2000.
  14. A. L. S. Vanz, G. Renard, M. S. Palma et al., “Human granulocyte colony stimulating factor (hG-CSF): cloning, overexpression, purification and characterization,” Microbial Cell Factories, vol. 7, article 13, 2008. View at Publisher · View at Google Scholar · View at Scopus
  15. D. R. Barreda, P. C. Hanington, and M. Belosevic, “Regulation of myeloid development and function by colony stimulating factors,” Developmental and Comparative Immunology, vol. 28, no. 5, pp. 509–554, 2004. View at Publisher · View at Google Scholar · View at Scopus
  16. L. J. Bendall and K. F. Bradstock, “G-CSF: from granulopoietic stimulant to bone marrow stem cell mobilizing agent,” Cytokine and Growth Factor Reviews, vol. 25, no. 4, pp. 355–367, 2014. View at Publisher · View at Google Scholar · View at Scopus
  17. A. Schneider, C. Krüger, T. Steigleder et al., “The hematopoietic factor G-CSF is a neuronal ligand that counteracts programmed cell death and drives neurogenesis,” The Journal of Clinical Investigation, vol. 115, no. 8, pp. 2083–2098, 2005. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Sell, “Heterogeneity and plasticity of hepatocyte lineage cells,” Hepatology, vol. 33, no. 3, pp. 738–750, 2001. View at Publisher · View at Google Scholar · View at Scopus
  19. C. K. Kim, C. H. Lee, S.-B. Lee, and J.-W. Oh, “Simplified large-scale refolding, purification, and characterization of recombinant human granulocyte-colony stimulating factor in Escherichia coli,” PLoS ONE, vol. 8, no. 11, Article ID e80109, 2013. View at Publisher · View at Google Scholar · View at Scopus
  20. S. A. Dehaghani, V. Babaeipour, M. R. Mofid, A. Divsalar, and F. Faraji, “An efficient purification method for high recovery of recombinant human granulocyte colony stimulating factor from recombinant E. coli,” International Journal of Environmental Science and Development, vol. 1, no. 2, pp. 111–114, 2010. View at Publisher · View at Google Scholar
  21. X.-Z. Zhang and Y.-H. P. Zhang, “Simple, fast and high-efficiency transformation system for directed evolution of cellulase in Bacillus subtilis,” Microbial Biotechnology, vol. 4, no. 1, pp. 98–105, 2011. View at Publisher · View at Google Scholar · View at Scopus
  22. S. Ahmad, H. Ma, M. W. Akhtar, Y.-H. P. Zhang, and X.-Z. Zhang, “Directed evolution of Clostridium phytofermentans glycoside hydrolase family 9 endoglucanase for enhanced specific activity on solid cellulosic substrate,” Bioenergy Research, vol. 7, no. 1, pp. 381–388, 2014. View at Publisher · View at Google Scholar · View at Scopus
  23. C. You, X.-Z. Zhang, N. Sathitsuksanoh, L. R. Lynd, and Y.-H. Percival Zhang, “Enhanced microbial utilization of recalcitrant cellulose by an ex vivo cellulosome-microbe complex,” Applied and Environmental Microbiology, vol. 78, no. 5, pp. 1437–1444, 2012. View at Publisher · View at Google Scholar · View at Scopus
  24. J. Sambrook and D. W. Russel, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA, 3rd edition, 2001.
  25. M. M. Bradford, “Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 248–254, 1976. View at Publisher · View at Google Scholar · View at Scopus
  26. G. Bohm, R. Muhr, and R. Jaenicke, “Quantitative analysis of protein far UV circular dichroism spectra by neural networks,” Protein Engineering, vol. 5, no. 3, pp. 191–195, 1992. View at Publisher · View at Google Scholar · View at Scopus
  27. B. Wittman, J. Horan, and G. H. Lyman, “Prophylactic colony-stimulating factors in children receiving myelosuppressive chemotherapy: a meta-analysis of randomized controlled trials,” Cancer Treatment Reviews, vol. 32, no. 4, pp. 289–303, 2006. View at Publisher · View at Google Scholar · View at Scopus
  28. R. García-Carbonero, J. I. Mayordomo, M. V. Tornamira et al., “Granulocyte colony-stimulating factor in the treatment of high-risk febrile neutropenia: a multicenter randomized trial,” Journal of the National Cancer Institute, vol. 93, no. 1, pp. 31–38, 2001. View at Publisher · View at Google Scholar · View at Scopus
  29. A. Apte-Deshpande, S. Somani, G. Mandal, S. Soorapaneni, and S. Padmanabhan, “Over expression and analysis of O-glycosylated recombinant human granulocyte colony stimulating factor in Pichia pastoris using Agilent 2100 Bioanalyzer,” Journal of Biotechnology, vol. 143, no. 1, pp. 44–50, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. A. Saeedinia, M. Shamsara, A. Bahrami et al., “Heterologous expression of human granulocyte-colony stimulating factor in Pichia pastoris,” Biotechnology, vol. 7, no. 3, pp. 569–573, 2008. View at Publisher · View at Google Scholar · View at Scopus
  31. M. A. Lasnik, V. G. Porekar, and A. Štalc, “Human granulocyte colony stimulating factor (hG-CSF) expressed by methylotrophic yeast Pichia pastoris,” Pflügers Archiv, vol. 442, no. 6, pp. R184–R186, 2001. View at Publisher · View at Google Scholar · View at Scopus
  32. N. Kubota, T. Orita, K. Hattori, M. Oh-Eda, N. Ochi, and T. Yamazaki, “Structural characterization of natural and recombinant human granulocyte colony-stimulating factors,” Journal of Biochemistry, vol. 107, no. 3, pp. 486–492, 1990. View at Google Scholar · View at Scopus
  33. F. R. Gomes, A. C. Maluenda, J. O. Tápias et al., “Expression of recombinant human mutant granulocyte colony stimulating factor (Nartograstim) in Escherichia coli,” World Journal of Microbiology and Biotechnology, vol. 28, no. 7, pp. 2593–2600, 2012. View at Publisher · View at Google Scholar · View at Scopus
  34. P. Gascon, “Presently available biosimilars in hematology-oncology: G-CSF,” Targeted Oncology, vol. 7, supplement 1, pp. S29–S34, 2012. View at Publisher · View at Google Scholar · View at Scopus
  35. U. Brockmeier, New Strategies to Optimize the Secretion Capacity for Heterologous Proteins in Bacillus Subtilis, Biowissenschaften der Ruhr-Universitat Bochum, 2006.
  36. K. Manabe, Y. Kageyama, M. Tohata, K. Ara, K. Ozaki, and N. Ogasawara, “High external pH enables more efficient secretion of alkaline α-amylase AmyK38 by Bacillus subtilis,” Microbial Cell Factories, vol. 11, article 74, 2012. View at Publisher · View at Google Scholar · View at Scopus
  37. T. Morimoto, R. Kadoya, K. Endo et al., “Enhanced recombinant protein productivity by genome reduction in Bacillus subtilis,” DNA Research, vol. 15, no. 2, pp. 73–81, 2008. View at Publisher · View at Google Scholar · View at Scopus
  38. K. Ara, K. Ozaki, K. Nakamura, K. Yamane, J. Sekiguchi, and N. Ogasawara, “Bacillus minimum genome factory: effective utilization of microbial genome information,” Biotechnology and Applied Biochemistry, vol. 46, no. 3, pp. 169–178, 2007. View at Publisher · View at Google Scholar · View at Scopus
  39. C.-K. Yang, H. E. Ewis, X. Zhang et al., “Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis,” Journal of Bacteriology, vol. 193, no. 20, pp. 5607–5615, 2011. View at Publisher · View at Google Scholar · View at Scopus
  40. D. A. Parry, E. Minasian, and S. J. Leach, “Conformational homologies among cytokines: interleukins and colony stimulating factors,” Journal of Molecular Recognition, vol. 1, no. 3, pp. 107–110, 1988. View at Publisher · View at Google Scholar · View at Scopus