Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2015, Article ID 767183, 11 pages
http://dx.doi.org/10.1155/2015/767183
Research Article

Cloning and Expression of Synthetic Genes Encoding the Broad Antimicrobial Spectrum Bacteriocins SRCAM 602, OR-7, E-760, and L-1077, by Recombinant Pichia pastoris

Departamento de Nutrición, Bromatología y Tecnología de los Alimentos, Facultad de Veterinaria, Universidad Complutense de Madrid (UCM), Avenida Puerta de Hierro, s/n, 28040 Madrid, Spain

Received 30 July 2014; Accepted 2 November 2014

Academic Editor: J. Eleazar Barboza-Corona

Copyright © 2015 Sara Arbulu 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. C. T. Lohans and J. C. Vederas, “Development of class IIa bacteriocins as therapeutic agents,” International Journal of Microbiology, vol. 2012, Article ID 386410, 13 pages, 2012. View at Publisher · View at Google Scholar · View at Scopus
  2. P. D. Cotter, R. P. Ross, and C. Hill, “Bacteriocins-a viable alternative to antibiotics?” Nature Reviews Microbiology, vol. 11, no. 2, pp. 95–105, 2013. View at Publisher · View at Google Scholar · View at Scopus
  3. S. Yang, Y. Kuang, H. Li et al., “Enhanced production of recombinant secretory proteins in Pichia pastoris by optimizing Kex2 P1’ site,” PLoS ONE, vol. 8, no. 9, Article ID e75347, 2013. View at Publisher · View at Google Scholar · View at Scopus
  4. P. D. Cotter, C. Hill, and R. P. Ross, “Food microbiology: bacteriocins: developing innate immunity for food,” Nature Reviews Microbiology, vol. 3, no. 10, pp. 777–788, 2005. View at Publisher · View at Google Scholar · View at Scopus
  5. D. Drider, G. Fimland, Y. Héchard, L. M. McMullen, and H. Prévost, “The continuing story of class IIa bacteriocins,” Microbiology and Molecular Biology Reviews, vol. 70, no. 2, pp. 564–582, 2006. View at Publisher · View at Google Scholar · View at Scopus
  6. J. Borrero, J. J. Jiménez, L. Gútiez, C. Herranz, L. M. Cintas, and P. E. Hernández, “Protein expression vector and secretion signal peptide optimization to drive the production, secretion, and functional expression of the bacteriocin enterocin A in lactic acid bacteria,” Journal of Biotechnology, vol. 156, no. 1, pp. 76–86, 2011. View at Publisher · View at Google Scholar · View at Scopus
  7. N. S. Parachin, K. C. Mulder, A. A. B. Viana, S. C. Dias, and O. L. Franco, “Expression systems for heterologous production of antimicrobial peptides,” Peptides, vol. 38, no. 2, pp. 446–456, 2012. View at Publisher · View at Google Scholar · View at Scopus
  8. J. J. Jiménez, J. Borrero, D. B. Diep et al., “Cloning, production, and functional expression of the bacteriocin sakacin A (SakA) and two SakA-derived chimeras in lactic acid bacteria (LAB) and the yeasts Pichia pastoris and Kluyveromyces lactis,” Journal of Industrial Microbiology & Biotechnology, vol. 40, no. 9, pp. 977–993, 2013. View at Publisher · View at Google Scholar · View at Scopus
  9. M. Gao and Z. Shi, “Process control and optimization for heterologous protein production by methylotrophic pichia pastoris,” Chinese Journal of Chemical Engineering, vol. 21, no. 2, pp. 216–226, 2013. View at Publisher · View at Google Scholar · View at Scopus
  10. M. Ahmad, M. Hirz, H. Pichler, and H. Schwab, “Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production,” Applied Microbiology and Biotechnology, vol. 98, pp. 5301–5317, 2014. View at Publisher · View at Google Scholar · View at Scopus
  11. J. Borrero, G. Kunze, J. Jiménez et al., “Cloning, production, and functional expression of the bacteriocin enterocin A, produced by Enterococcus faecium T136, by the Yeasts Pichia pastoris, Kluyveromyces lactis, Hansenula polymorpha, and Arxula adeninivorans,” Applied and Environmental Microbiology, vol. 78, no. 16, pp. 5956–5961, 2012. View at Publisher · View at Google Scholar · View at Scopus
  12. J. J. Jiménez, J. Borrero, L. Gútiez et al., “Use of synthetic genes for cloning, production and functional expression of the bacteriocins enterocin A and bacteriocin E 50-52 by Pichia pastoris and Kluyveromyces lactis,” Molecular Biotechnology, vol. 56, no. 6, pp. 571–583, 2014. View at Publisher · View at Google Scholar · View at Scopus
  13. R. A. J. Darby, S. P. Cartwright, M. V. Dilworth, and R. M. Bill, “Which yeast species shall i choose? Saccharomyces cerevisiae versus Pichia pastoris,” Methods in Molecular Biology, vol. 866, pp. 11–23, 2012. View at Publisher · View at Google Scholar · View at Scopus
  14. F. Öberg, J. Sjöhamn, M. T. Conner, R. M. Bill, and K. Hedfalk, “Improving recombinant eukaryotic membrane protein yields in Pichia pastoris: the importance of codon optimization and clone selection,” Molecular Membrane Biology, vol. 28, no. 6, pp. 398–411, 2011. View at Publisher · View at Google Scholar · View at Scopus
  15. N. J. Stern, E. A. Svetoch, B. V. Eruslanov et al., “Paenibacillus polymyxa purified bacteriocin to control Campylobacter jejuni in chickens,” Journal of Food Protection, vol. 68, no. 7, pp. 1450–1453, 2005. View at Google Scholar · View at Scopus
  16. E. A. Svetoch, N. J. Stern, B. V. Eruslanov et al., “Isolation of Bacillus circulans and Paenibacillus polymyxa strains inhibitory to Campylobacter jejuni and characterization of associated bacteriocins,” Journal of Food Protection, vol. 68, no. 1, pp. 11–17, 2005. View at Google Scholar · View at Scopus
  17. N. J. Stern, E. A. Svetoch, B. V. Eruslanov et al., “Isolation of a Lactobacillus salivarius strain and purification of its bacteriocin, which is inhibitory to Campylobacter jejuni in the chicken gastrointestinal system,” Antimicrobial Agents and Chemotherapy, vol. 50, no. 9, pp. 3111–3116, 2006. View at Publisher · View at Google Scholar · View at Scopus
  18. E. A. Svetoch, B. V. Eruslanov, V. P. Levchuk et al., “Isolation of Lactobacillus salivarius 1077 (NRRL B-50053) and characterization of its bacteriocin, including the antimicrobial activity spectrum,” Applied and Environmental Microbiology, vol. 77, no. 8, pp. 2749–2754, 2011. View at Publisher · View at Google Scholar · View at Scopus
  19. J. E. Line, E. A. Svetoch, B. V. Eruslanov et al., “Isolation and purification of enterocin E-760 with broad antimicrobial activity against Gram-positive and Gram-negative bacteria,” Antimicrobial Agents and Chemotherapy, vol. 52, no. 3, pp. 1094–1100, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. E. A. Svetoch, B. V. Eruslanov, V. V. Perelygin et al., “Diverse antimicrobial killing by Enterococcus faecium E 50-52 bacteriocin,” Journal of Agricultural and Food Chemistry, vol. 56, no. 6, pp. 1942–1948, 2008. View at Publisher · View at Google Scholar · View at Scopus
  21. E. A. Svetoch and N. J. Stern, “Bacteriocins to control Campylobacter spp. in poultry-a review,” Poultry Science, vol. 89, no. 8, pp. 1763–1768, 2010. View at Publisher · View at Google Scholar · View at Scopus
  22. J. Gutiérrez, R. Criado, M. Martín, C. Herranz, L. M. Cintas, and P. E. Hernández, “Production of enterocin P, an antilisterial pediocin-like bacteriocin from Enterococcus faecium P13, in Pichia pastons,” Antimicrobial Agents and Chemotherapy, vol. 49, no. 7, pp. 3004–3008, 2005. View at Publisher · View at Google Scholar · View at Scopus
  23. A. Shevchenko, A. Loboda, W. Ens, and K. G. Standing, “MALDI quadrupole time-of-flight mass spectrometry: a powerful tool for proteomic research,” Analytical Chemistry, vol. 72, no. 9, pp. 2132–2141, 2000. View at Publisher · View at Google Scholar · View at Scopus
  24. World Health Organization (WHO), “Antimicrobial resistance: global report on surveillance 2014,” http://www.searo.who.int/thailand/publications/2013/9789241564748/en/.
  25. E. Böer, G. Steinborn, G. Kunze, and G. Gellissen, “Yeast expression platforms,” Applied Microbiology and Biotechnology, vol. 77, no. 3, pp. 513–523, 2007. View at Publisher · View at Google Scholar · View at Scopus
  26. J. M. Cregg, J. L. Cereghino, J. Shi, and D. R. Higgins, “Recombinant protein expression in Pichia pastoris,” Applied Biochemistry and Biotechnology—Part B Molecular Biotechnology, vol. 16, no. 1, pp. 23–52, 2000. View at Google Scholar · View at Scopus
  27. O. J. Burrowes, G. Diamond, and T. C. Lee, “Recombinant expression of pleurocidin cDNA using the Pichia pastoris expression system,” Journal of Biomedicine and Biotechnology, vol. 2005, no. 4, pp. 374–384, 2005. View at Publisher · View at Google Scholar · View at Scopus
  28. K. R. Love, T. J. Politano, V. Panagiotou, B. Jiang, T. A. Stadheim, and J. C. Love, “Systematic single-cell analysis of pichia pastoris reveals secretory capacity limits productivity,” PLoS ONE, vol. 7, no. 6, Article ID e37915, 2012. View at Publisher · View at Google Scholar · View at Scopus
  29. H. A. Kang, E.-S. Choi, W.-K. Hong et al., “Proteolytic stability of recombinant human serum albumin secreted in the yeast Saccharomyces cerevisiae,” Applied Microbiology and Biotechnology, vol. 53, no. 5, pp. 575–582, 2000. View at Publisher · View at Google Scholar · View at Scopus
  30. M. W. T. Werten and F. A. De Wolf, “Reduced proteolysis of secreted gelatin and Yps1-mediated α-factor leader processing in a Pichia pastoris kex2 disruptant,” Applied and Environmental Microbiology, vol. 71, no. 5, pp. 2310–2317, 2005. View at Publisher · View at Google Scholar · View at Scopus
  31. Z. Ni, X. Zhou, X. Sun, Y. Wang, and Y. Zhang, “Decrease of hirudin degradation by deleting the KEX1 gene in recombinant Pichia pastoris,” Yeast, vol. 25, no. 1, pp. 1–8, 2008. View at Publisher · View at Google Scholar · View at Scopus
  32. J. Borrero, D. A. Brede, M. Skaugen et al., “Characterization of garvicin ML, a novel circular bacteriocin produced by Lactococcus garvieae DCC43, isolated from mallard ducks (Anas platyrhynchos),” Applied and Environmental Microbiology, vol. 77, no. 1, pp. 369–373, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. Y. Zhao and O. N. Jensen, “Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniques,” Proteomics, vol. 9, no. 20, pp. 4632–4641, 2009. View at Publisher · View at Google Scholar · View at Scopus
  34. B. Gasser, M. Saloheimo, U. Rinas et al., “Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview,” Microbial Cell Factories, vol. 7, article 11, 2008. View at Publisher · View at Google Scholar · View at Scopus
  35. A. Stolz and D. H. Wolf, “Endoplasmic reticulum associated protein degradation: a chaperone assisted journey to hell,” Biochimica et Biophysica Acta—Molecular Cell Research, vol. 1803, no. 6, pp. 694–705, 2010. View at Publisher · View at Google Scholar · View at Scopus
  36. E. Breukink, I. Wiedemann, C. van Kraaij, O. P. Kuipers, H.-G. Sahl, and B. de Kruijff, “Use of the cell wail precursor lipid II by a pore-forming peptide antibiotic,” Science, vol. 286, no. 5448, pp. 2361–2364, 1999. View at Publisher · View at Google Scholar · View at Scopus
  37. D. B. Diep, M. Skaugen, Z. Salehian, H. Holo, and I. F. Nes, “Common mechanisms of target cell recognition and immunity for class II bacteriocins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 7, pp. 2384–2389, 2007. View at Publisher · View at Google Scholar · View at Scopus
  38. M. Kjos, J. Borrero, M. Opsata et al., “Target recognition, resistance, immunity and genome mining of class II bacteriocins from Gram-positive bacteria,” Microbiology, vol. 157, no. 12, pp. 3256–3267, 2011. View at Publisher · View at Google Scholar · View at Scopus
  39. M. Phelan, A. Aherne, R. J. FitzGerald, and N. M. O'Brien, “Casein-derived bioactive peptides: biological effects, industrial uses, safety aspects and regulatory status,” International Dairy Journal, vol. 19, no. 11, pp. 643–654, 2009. View at Publisher · View at Google Scholar · View at Scopus
  40. G. D. Brand, M. T. Q. Magalhães, M. L. P. Tinoco et al., “Probing protein sequences as sources for encrypted antimicrobial peptides,” PLoS ONE, vol. 7, no. 9, Article ID e45848, 2012. View at Publisher · View at Google Scholar · View at Scopus
  41. E. A. Svetoch, V. P. Levchuk, V. D. Pokhilenko et al., “Inactivating methicillin-resistant Staphylococcus aureus and other pathogens by use of bacteriocins OR-7 and E 50-52,” Journal of Clinical Microbiology, vol. 46, no. 11, pp. 3863–3865, 2008. View at Publisher · View at Google Scholar · View at Scopus
  42. J. Sánchez, J. Borrero, B. Gómez-Sala et al., “Cloning and heterologous production of hiracin JM79, a Sec-dependent bacteriocin produced by Enterococcus hirae DCH5, in lactic acid bacteria and Pichia pastoris,” Applied and Environmental Microbiology, vol. 74, no. 8, pp. 2471–2479, 2008. View at Publisher · View at Google Scholar · View at Scopus
  43. C. T. Lohans, Z. Huang, M. J. Van Belkum et al., “Structural characterization of the highly cyclized lantibiotic paenicidin A via a partial desulfurization/reduction strategy,” Journal of the American Chemical Society, vol. 134, no. 48, pp. 19540–19543, 2012. View at Publisher · View at Google Scholar · View at Scopus
  44. C. T. Lohans, M. J. Van Belkum, S. A. Cochrane et al., “Biochemical, structural, and genetic characterization of tridecaptin A1, an antagonist of Campylobacter jejuni,” ChemBioChem, vol. 15, no. 2, pp. 243–249, 2014. View at Publisher · View at Google Scholar · View at Scopus