Table of Contents Author Guidelines Submit a Manuscript
Table of Contents Alerts

To receive news and publication updates for International Journal of Microbiology, enter your email address in the box below.

International Journal of Microbiology
Volume 2012 (2012), Article ID 101989, 8 pages
http://dx.doi.org/10.1155/2012/101989
Review Article

Coleopteran Antimicrobial Peptides: Prospects for Clinical Applications

Monde Ntwasa,1 Akira Goto,2 and Shoichiro Kurata2

1School of Molecular and Cell Biology, University of the Witwatersrand, Wits 2050, South Africa
2Graduate School of Pharmaceutical Sciences, Tohoku University, Aoba 6-3, Aramaki, Aoba-ku, Sendai 980-8578, Japan

Received 8 August 2011; Revised 2 November 2011; Accepted 5 December 2011

Academic Editor: Paul Cotter

Copyright © 2012 Monde Ntwasa 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. D. Tautz, “Insects on the rise,” Trends in Genetics, vol. 18, no. 4, pp. 179–180, 2002. View at Publisher · View at Google Scholar · View at Scopus
  2. S. Richards, R. A. Gibbs, G. M. Weinstock et al., “The genome of the model beetle and pest Tribolium castaneum,” Nature, vol. 452, no. 7190, pp. 949–955, 2008. View at Publisher · View at Google Scholar · View at Scopus
  3. J. A. Hoffmann, “The immune response of Drosophila,” Nature, vol. 426, no. 6962, pp. 33–38, 2003. View at Publisher · View at Google Scholar · View at Scopus
  4. J. A. Hoffmann, “Primitive immune systems,” Immunological Reviews, vol. 198, pp. 5–9, 2004. View at Publisher · View at Google Scholar · View at Scopus
  5. J. Savard, D. Tautz, and M. J. Lercher, “Genome-wide acceleration of protein evolution in flies (Diptera),” BMC Evolutionary Biology, vol. 6, p. 7, 2006. View at Publisher · View at Google Scholar · View at Scopus
  6. M. van der Zee, R. N. da Fonseca, and S. Roth, “TGFβ signaling in Tribolium: vertebrate-like components in a beetle,” Development Genes and Evolution, vol. 218, no. 3-4, pp. 203–213, 2008. View at Publisher · View at Google Scholar · View at Scopus
  7. P. Bulet and R. Stöcklin, “Insect antimicrobial peptides: structures, properties and gene regulation,” Protein and Peptide Letters, vol. 12, no. 1, pp. 3–11, 2005. View at Publisher · View at Google Scholar · View at Scopus
  8. P. Bulet, R. Stöcklin, and L. Menin, “Anti-microbial peptides: from invertebrates to vertebrates,” Immunological Reviews, vol. 198, no. 1, pp. 169–184, 2004. View at Publisher · View at Google Scholar · View at Scopus
  9. A. Tossi, L. Sandri, and A. Giangaspero, “Amphipathic, α-helical antimicrobial peptides,” Peptide Science, vol. 55, no. 1, pp. 4–30, 2000. View at Publisher · View at Google Scholar · View at Scopus
  10. Y. Shai, “Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides,” Biochimica et Biophysica Acta, vol. 1462, no. 1-2, pp. 55–70, 1999. View at Publisher · View at Google Scholar · View at Scopus
  11. Z. Oren and Y. Shai, “Mode of action of linear amphipathic α-helical antimicrobial peptides,” Peptide Science, vol. 47, no. 6, pp. 451–463, 1998. View at Google Scholar · View at Scopus
  12. K. V. R. Reddy, R. D. Yedery, and C. Aranha, “Antimicrobial peptides: premises and promises,” International Journal of Antimicrobial Agents, vol. 24, no. 6, pp. 536–547, 2004. View at Publisher · View at Google Scholar · View at Scopus
  13. R. E. Dean, L. M. O'Brien, J. E. Thwaite, M. A. Fox, H. Atkins, and D. O. Ulaeto, “A carpet-based mechanism for direct antimicrobial peptide activity against vaccinia virus membranes,” Peptides, vol. 31, no. 11, pp. 1966–1972, 2010. View at Publisher · View at Google Scholar · View at Scopus
  14. K. Takeuchi, H. Takahashi, M. Sugai et al., “Channel-forming membrane permeabilization by an antibacterial protein, sapecin,” Journal of Biological Chemistry, vol. 279, no. 6, pp. 4981–4987, 2004. View at Publisher · View at Google Scholar · View at Scopus
  15. K. Matsuzaki, “Magainins as paradigm for the mode of action of pore forming polypeptides,” Biochimica et Biophysica Acta, vol. 1376, no. 3, pp. 391–400, 1998. View at Publisher · View at Google Scholar · View at Scopus
  16. K. A. Brogden, “Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?” Nature Reviews Microbiology, vol. 3, no. 3, pp. 238–250, 2005. View at Publisher · View at Google Scholar · View at Scopus
  17. R. Mani, S. D. Cady, M. Tang, A. J. Waring, R. I. Lehrer, and M. Hong, “Membrane-dependent oligomeric structure and pore formation of a β-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 44, pp. 16242–16247, 2006. View at Publisher · View at Google Scholar · View at Scopus
  18. A. Bellemare, N. Vernoux, S. Morin, S. M. Gagné, and Y. Bourbonnais, “Structural and antimicrobial properties of human pre-elafin/trappin-2 and derived peptides against Pseudomonas aeruginosa,” BMC Microbiology, vol. 10, no. 1, p. 253, 2010. View at Publisher · View at Google Scholar · View at Scopus
  19. C. B. Park, H. S. Kim, and S. C. Kim, “Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions,” Biochemical and Biophysical Research Communications, vol. 244, no. 1, pp. 253–257, 1998. View at Publisher · View at Google Scholar · View at Scopus
  20. D. Mania, K. Hilpert, S. Ruden, R. Fischer, and N. Takeshita, “Screening for antifungal peptides and their modes of action in Aspergillus nidulans,” Applied and Environmental Microbiology, vol. 76, no. 21, pp. 7102–7108, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. J. D. F. Hale and R. E. W. Hancock, “Alternative mechanisms of action of cationic antimicrobial peptides on bacteria,” Expert Review of Anti-Infective Therapy, vol. 5, no. 6, pp. 951–959, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. Z. Zou, J. D. Evans, Z. Lu et al., “Comparative genomic analysis of the Tribolium immune system,” Genome Biology, vol. 8, no. 8, p. R177, 2007. View at Publisher · View at Google Scholar · View at Scopus
  23. R. Bals and J. M. Wilson, “Cathelicidins—a family of multifunctional antimicrobial peptides,” Cellular and Molecular Life Sciences, vol. 60, no. 4, pp. 711–720, 2003. View at Publisher · View at Google Scholar · View at Scopus
  24. M. G. Scott and R. E. W. Hancock, “Cationic antimicrobial peptides and their multifunctional role in the immune system,” Critical Reviews in Immunology, vol. 20, no. 5, pp. 407–431, 2000. View at Google Scholar · View at Scopus
  25. J. E. Meyer and J. Harder, “Antimicrobial peptides in oral cancer,” Current Pharmaceutical Design, vol. 13, no. 30, pp. 3119–3130, 2007. View at Publisher · View at Google Scholar · View at Scopus
  26. A. F. Gombart, N. Borregaard, and H. P. Koeffler, “Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly up-regulated in myeloid cells by 1,25-dihydroxyvitamin D3,” FASEB Journal, vol. 19, no. 9, pp. 1067–1077, 2005. View at Publisher · View at Google Scholar · View at Scopus
  27. B. de Yang, Q. Chen, A. P. Schmidt et al., “LL-37, the neutrophil granule-and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells,” Journal of Experimental Medicine, vol. 192, no. 7, pp. 1069–1074, 2000. View at Publisher · View at Google Scholar · View at Scopus
  28. F. Schweizer, “Cationic amphiphilic peptides with cancer-selective toxicity,” European Journal of Pharmacology, vol. 625, no. 1–3, pp. 190–194, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. A. T. Y. Yeung, S. L. Gellatly, and R. E. W. Hancock, “Multifunctional cationic host defence peptides and their clinical applications,” Cellular and Molecular Life Sciences, vol. 68, no. 13, pp. 2161–2176, 2011. View at Publisher · View at Google Scholar
  30. E. Andrès and J. L. Dimarcq, “Clinical development of antimicrobial peptides,” International Journal of Antimicrobial Agents, vol. 25, no. 5, pp. 448–449, 2005. View at Publisher · View at Google Scholar · View at Scopus
  31. H. Suttmann, M. Retz, F. Paulsen et al., “Antimicrobial peptides of the Cecropin-family show potent antitumor activity against bladder cancer cells,” BMC Urology, vol. 8, no. 1, p. 5, 2008. View at Publisher · View at Google Scholar · View at Scopus
  32. D. Yang, O. Chertov, S. N. Bykovskaia et al., “β-Defensins: linking innate and adaptive immunity through dendritic and T cell CCR6,” Science, vol. 286, no. 5439, pp. 525–528, 1999. View at Publisher · View at Google Scholar · View at Scopus
  33. F. Niyonsaba, H. Ushio, M. Hara et al., “Antimicrobial peptides human β-defensins and cathelicidin LL-37 induce the secretion of a pruritogenic cytokine IL-31 by human mast cells,” Journal of Immunology, vol. 184, no. 7, pp. 3526–3534, 2010. View at Publisher · View at Google Scholar · View at Scopus
  34. S. Dressel, J. Harder, J. Cordes et al., “Differential expression of antimicrobial peptides in margins of chronic wounds,” Experimental Dermatology, vol. 19, no. 7, pp. 628–632, 2010. View at Publisher · View at Google Scholar · View at Scopus
  35. L. Zhang and T. J. Falla, “Cosmeceuticals and peptides,” Clinics in Dermatology, vol. 27, no. 5, pp. 485–494, 2009. View at Publisher · View at Google Scholar · View at Scopus
  36. B. Altincicek, E. Knorr, and A. Vilcinskas, “Beetle immunity: identification of immune-inducible genes from the model insect Tribolium castaneum,” Developmental and Comparative Immunology, vol. 32, no. 5, pp. 585–595, 2008. View at Publisher · View at Google Scholar · View at Scopus
  37. S. Seebah, A. Suresh, S. Zhuo et al., “Defensins knowledgebase: a manually curated database and information source focused on the defensins family of antimicrobial peptides,” Nucleic Acids Research, vol. 35, supplement 1, pp. D265–D268, 2007. View at Publisher · View at Google Scholar · View at Scopus
  38. M. Hedengren, K. Borge, and D. Hultmark, “Expression and evolution of the Drosophila Attacin/Diptericin gene family,” Biochemical and Biophysical Research Communications, vol. 279, no. 2, pp. 574–581, 2000. View at Publisher · View at Google Scholar · View at Scopus
  39. A. Sagisaka, A. Miyanoshita, J. Ishibashi, and M. Yamakawa, “Purification, characterization and gene expression of a glycine and proline-rich antibacterial protein family from larvae of a beetle, Allomyrina dichotoma,” Insect Molecular Biology, vol. 10, no. 4, pp. 293–302, 2001. View at Publisher · View at Google Scholar · View at Scopus
  40. C. Anselme, V. Pérez-Brocal, A. Vallier et al., “Identification of the weevil immune genes and their expression in the bacteriome tissue,” BMC Biology, vol. 6, no. 1, p. 43, 2008. View at Publisher · View at Google Scholar · View at Scopus
  41. Y. Yu, J.-W. Park, H.-M. Kwon et al., “Diversity of innate immune recognition mechanism for bacterial polymeric meso-diaminopimelic acid-type peptidoglycan in insects,” Journal of Biological Chemistry, vol. 285, no. 43, pp. 32937–32945, 2010. View at Publisher · View at Google Scholar · View at Scopus
  42. F. Barbault, C. Landon, M. Guenneugues et al., “Solution structure of Alo-3: a new knottin-type antifungal peptide from the insect Acrocinus longimanus,” Biochemistry, vol. 42, no. 49, pp. 14434–14442, 2003. View at Publisher · View at Google Scholar · View at Scopus
  43. J. S. Hwang, J. Lee, B. Hwang et al., “Isolation and characterization of psacotheasin, a novel knottin-type antimicrobial peptide, from Psacothea hilaris,” Journal of Microbiology and Biotechnology, vol. 20, no. 4, pp. 708–711, 2010. View at Publisher · View at Google Scholar · View at Scopus
  44. A. Saito, K. Ueda, M. Imamura et al., “Purification and cDNA cloning of a cecropin from the longicorn beetle, Acalolepta luxuriosa,” Comparative Biochemistry and Physiology B, vol. 142, no. 3, pp. 317–323, 2005. View at Publisher · View at Google Scholar · View at Scopus
  45. B. Hwang, J. S. Hwang, J. Lee, and D. G. Lee, “Antifungal properties and mode of action of psacotheasin, a novel knottin-type peptide derived from Psacothea hilaris,” Biochemical and Biophysical Research Communications, vol. 400, no. 3, pp. 352–357, 2010. View at Publisher · View at Google Scholar · View at Scopus
  46. S. Lu, P. Deng, X. Liu et al., “Solution structure of the major α-amylase inhibitor of the crop plant amaranth,” Journal of Biological Chemistry, vol. 274, no. 29, pp. 20473–20478, 1999. View at Publisher · View at Google Scholar · View at Scopus
  47. B. Hwang, J. S. Hwang, J. Lee, and D. G. Lee, “The antimicrobial peptide, psacotheasin induces reactive oxygen species and triggers apoptosis in Candida albicans,” Biochemical and Biophysical Research Communications, vol. 405, no. 2, pp. 267–271, 2011. View at Publisher · View at Google Scholar
  48. R. E. Lewis and M. E. Klepser, “The changing face of nosocomial candidemia: epidemiology, resistance, and drug therapy,” American Journal of Health-System Pharmacy, vol. 56, no. 6, pp. 525–533, 1999. View at Google Scholar · View at Scopus
  49. M. H. Nguyen, J. E. Peacock, A. J. Morris et al., “The changing face of candidemia: emergence of non-Candida albicans species and antifungal resistance,” American Journal of Medicine, vol. 100, no. 6, pp. 617–623, 1996. View at Publisher · View at Google Scholar · View at Scopus
  50. Z. Wang and G. Wang, “APD: the antimicrobial peptide database,” Nucleic Acids Research, vol. 32, supplement 1, pp. D590–D592, 2004. View at Google Scholar · View at Scopus
  51. G. Wang, X. Li, and Z. Wang, “APD2: the updated antimicrobial peptide database and its application in peptide design,” Nucleic Acids Research, vol. 37, supplement 1, pp. D933–D937, 2009. View at Publisher · View at Google Scholar · View at Scopus
  52. Y. Gueguen, J. Garnier, L. Robert et al., “PenBase, the shrimp antimicrobial peptide penaeidin database: sequence-based classification and recommended nomenclature,” Developmental and Comparative Immunology, vol. 30, no. 3, pp. 283–288, 2006. View at Publisher · View at Google Scholar · View at Scopus
  53. L. M. Khanyile, R. Hull, and M. Ntwasa, “Dung beetle database: comparison with other invertebrate transcriptomes,” Bioinformation, vol. 3, no. 4, pp. 159–161, 2008. View at Google Scholar
  54. S. Lata, N. K. Mishra, and G. P. S. Raghava, “AntiBP2: improved version of antibacterial peptide prediction,” BMC Bioinformatics, vol. 11, no. 1, p. S19, 2010. View at Publisher · View at Google Scholar · View at Scopus
  55. S. Lata, B. K. Sharma, and G. P. S. Raghava, “Analysis and prediction of antibacterial peptides,” BMC Bioinformatics, vol. 8, p. 263, 2007. View at Publisher · View at Google Scholar · View at Scopus
  56. H. Vogel, C. Badapanda, and A. Vilcinskas, “Identification of immunity-related genes in the burying beetle Nicrophorus vespilloides by suppression subtractive hybridization,” Insect Molecular Biology, vol. 20, no. 6, pp. 787–800, 2011. View at Publisher · View at Google Scholar
  57. J.-W. Park, C.-H. Kim, J. Rui et al., Beetle Immunity Invertebrate Immunity, Springer, New York, NY, USA, 2010.
  58. A. Takehana, T. Katsuyama, T. Yano et al., “Overexpression of a pattern-recognition receptor, peptidoglycan-recognition protein-LE, activates imd/relish-mediated antibacterial defense and the prophenoloxidase cascade in Drosophila larvae,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 21, pp. 13705–13710, 2002. View at Publisher · View at Google Scholar · View at Scopus
  59. S. Shrestha and Y. Kim, “Activation of immune-associated phospholipase A2 is functionally linked to Toll/Imd signal pathways in the red flour beetle, Tribolium castaneum,” Developmental and Comparative Immunology, vol. 34, no. 5, pp. 530–537, 2010. View at Publisher · View at Google Scholar · View at Scopus
  60. J. S. Ju, M. H. Cho, L. Brade et al., “A novel 40-kDa protein containing six repeats of an epidermal growth factor-like domain functions as a pattern recognition protein for lipopolysaccharide,” Journal of Immunology, vol. 177, no. 3, pp. 1838–1845, 2006. View at Google Scholar · View at Scopus
  61. J. Wehkamp, E. F. Stange, and K. Fellermann, “Defensin-immunology in inflammatory bowel disease,” Gastroentérologie Clinique et Biologique, vol. 33, supplement 3, pp. S137–S144, 2009. View at Google Scholar
  62. M. E. Evans, D. J. Feola, and R. P. Rapp, “Polymyxin B sulfate and colistin: old antibiotics for emerging multiresistant gram-negative bacteria,” Annals of Pharmacotherapy, vol. 33, no. 9, pp. 960–967, 1999. View at Publisher · View at Google Scholar · View at Scopus
  63. A. K. Marr, W. J. Gooderham, and R. E. Hancock, “Antibacterial peptides for therapeutic use: obstacles and realistic outlook,” Current Opinion in Pharmacology, vol. 6, no. 5, pp. 468–472, 2006. View at Publisher · View at Google Scholar · View at Scopus
  64. S. A. Okorochenkov, G. A. Zheltukhina, and V. E. Nebol'sin, “Antimicrobial peptides: the mode of action and perspectives of practical application,” Biochemistry (Moscow) Supplement Series B, vol. 5, no. 2, pp. 95–102, 2011. View at Publisher · View at Google Scholar
  65. M. Zasloff, “Antimicrobial peptides of multicellular organisms,” Nature, vol. 415, no. 6870, pp. 389–395, 2002. View at Publisher · View at Google Scholar · View at Scopus
  66. R. E. W. Hancock, K. L. Brown, and N. Mookherjee, “Host defence peptides from invertebrates—emerging antimicrobial strategies,” Immunobiology, vol. 211, no. 4, pp. 315–322, 2006. View at Publisher · View at Google Scholar · View at Scopus