Broad activity against porcine bacterial pathogens displayed by two insect antimicrobial peptides moricin and cecropin B.

Han Hu, Chunmei Wang, Xiaozhen Guo, Wentao Li, Yang Wang, Qigai He
Author Information
  1. Han Hu: State Key Laboratory of Agricultural Microbiology, Division of Animal Infectious Disease, Huazhong Agricultural University, Wuhan, Hubei, China.

Abstract

In response to infection, insects produce a variety of antimicrobial peptides (AMPs) to kill the invading pathogens. To study their physicochemical properties and bioactivities for clinical and commercial use in the porcine industry, we chemically synthesized the mature peptides Bombyx mori moricin and Hyalophora cecropia cecropin B. In this paper, we described the antimicrobial activity of the two AMPs. Moricin exhibited antimicrobial activity on eight strains tested with minimal inhibitory concentration values (MICs) ranging between 8 and 128 μg/ml, while cecropin B mainly showed antimicrobial activity against the Gramnegative strains with MICs ranging from 0.5 to 16 μg/ml. Compared to the potent antimicrobial activity these two AMPs displayed against most of the bacterial pathogens tested, they exhibited limited hemolytic activity against porcine red blood cells. The activities of moricin and cecropin B against Haemophilus parasuis SH 0165 were studied in further detail. Transmission electron microscopy (TEM) of moricin and cecropin B treated H. parasuis SH 0165 indicated extensive damage to the membranes of the bacteria. Insights into the probable mechanism utilized by moricin and cecropin B to eliminate pathogens are also presented. The observations from this study are important for the future application of AMPs in the porcine industry.

References

  1. Eur J Biochem. 1982 Sep;127(1):207-17 [PMID: 7140755]
  2. Mol Cells. 2010 Apr;29(4):419-23 [PMID: 20213310]
  3. FEBS Lett. 2002 May 8;518(1-3):33-8 [PMID: 11997013]
  4. Ciba Found Symp. 1994;186:77-85; discussion 85-90 [PMID: 7768159]
  5. Proc Natl Acad Sci U S A. 1988 Jul;85(14):5072-6 [PMID: 2455891]
  6. Proc Natl Acad Sci U S A. 1985 Apr;82(8):2240-3 [PMID: 3857578]
  7. Mol Immunol. 2008 Jan;45(2):386-94 [PMID: 17658606]
  8. FEBS Lett. 1982 Jan 25;137(2):283-7 [PMID: 15768483]
  9. Biochim Biophys Acta. 1988 Apr 7;939(2):260-6 [PMID: 3128324]
  10. Biochim Biophys Acta. 2006 Sep;1758(9):1450-60 [PMID: 16989771]
  11. Biochem J. 1995 Sep 1;310 ( Pt 2):651-6 [PMID: 7654207]
  12. Biochim Biophys Acta. 2006 Sep;1758(9):1245-56 [PMID: 16697975]
  13. Eur J Biochem. 1980 May;106(1):7-16 [PMID: 7341234]
  14. Vet Microbiol. 2012 Apr 23;156(1-2):172-7 [PMID: 22104584]
  15. Biochem J. 2010 Apr 14;427(3):477-88 [PMID: 20187872]
  16. FEMS Microbiol Lett. 2002 Jan 10;206(2):143-9 [PMID: 11814654]
  17. Biochim Biophys Acta. 2005 Aug 31;1752(1):83-92 [PMID: 16115804]
  18. Biochemistry. 1995 Sep 12;34(36):11479-88 [PMID: 7547876]
  19. Clin Microbiol Rev. 2006 Jul;19(3):491-511 [PMID: 16847082]
  20. J Biol Chem. 1995 Dec 15;270(50):29923-7 [PMID: 8530391]
  21. Antimicrob Agents Chemother. 2010 Aug;54(8):3132-42 [PMID: 20530225]
  22. Microsc Res Tech. 2003 Dec 1;62(5):423-30 [PMID: 14601148]
  23. Nat Rev Microbiol. 2005 Mar;3(3):238-50 [PMID: 15703760]
  24. Biophys J. 1992 Dec;63(6):1623-31 [PMID: 1283347]
  25. Peptides. 2009 May;30(5):839-48 [PMID: 19428759]
  26. Cell Mol Life Sci. 2003 Mar;60(3):599-606 [PMID: 12737319]
  27. Int J Antimicrob Agents. 2007 Aug;30(2):134-42 [PMID: 17531447]
  28. Vet Microbiol. 2011 Jun 2;150(3-4):344-8 [PMID: 21411247]
  29. Antimicrob Agents Chemother. 1997 Aug;41(8):1738-42 [PMID: 9257752]
  30. Appl Environ Microbiol. 2010 Feb;76(3):769-75 [PMID: 19966019]
  31. Biochemistry. 2005 Jul 19;44(28):9804-16 [PMID: 16008365]

MeSH Term

Amino Acid Sequence
Animals
Anti-Infective Agents
Antimicrobial Cationic Peptides
Bacteria
Cell Membrane
Dose-Response Relationship, Drug
Erythrocytes
Haemophilus parasuis
Insect Proteins
Microscopy, Electron, Transmission
Molecular Sequence Data
Swine

Chemicals

Anti-Infective Agents
Antimicrobial Cationic Peptides
Insect Proteins
moricin protein, Bombyx mori
cecropin B protein, Insecta

Word Cloud

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