DOI QR코드

DOI QR Code

Development of a Novel Short Synthetic Antibacterial Peptide Derived from the Swallowtail Butterfly Papilio xuthus Larvae

  • Kim, Seong Ryul (Sericultural and Apicultural Materials Division, National Academy of Agricultural Science, RDA) ;
  • Choi, Kwang-Ho (Sericultural and Apicultural Materials Division, National Academy of Agricultural Science, RDA) ;
  • Kim, Kee-Young (Sericultural and Apicultural Materials Division, National Academy of Agricultural Science, RDA) ;
  • Kwon, Hye-Yong (Sericultural and Apicultural Materials Division, National Academy of Agricultural Science, RDA) ;
  • Park, Seung-Won (Department of Biomedical Science, Daegu Catholic University)
  • Received : 2020.03.06
  • Accepted : 2020.06.11
  • Published : 2020.09.28

Abstract

Insects possess biological defense systems that can effectively combat the invasion of external microorganisms and viruses, thereby supporting their survival in diverse environments. Antimicrobial peptides (AMPs) represent a fast-acting weapon against invading pathogens, including various bacterial or fungal strains. A 37-residue antimicrobial peptide, papiliocin, derived from the swallowtail butterfly Papilio xuthus larvae, showed significant antimicrobial activities against several human pathogenic bacterial and fungal strains. Jelleines, isolated as novel antibacterial peptides from the Royal Jelly (RJ) of bees, exhibit broad-spectrum protection against microbial infections. In this study, we developed a novel antimicrobial peptide, PAJE (RWKIFKKPFKISIHL-NH2), which is a hybrid peptide prepared by combining 1-7 amino acid residues (RWKIFKK-NH2) of papiliocin and 1-8 amino acid residues (PFKISIHL-NH2) of Jelleine-1 to alter length, charge distribution, net charge, volume, amphipaticity, and improve bacterial membrane interactions. This novel peptide exhibited increased hydrophobicity and net positive charge for binding effectively to the negatively charged membrane. PAJE demonstrated antimicrobial activity against both gram-negative and gram-positive bacteria, with very low toxicity to eukaryotic cells and an inexpensive process of synthesis. Collectively, these findings suggest that this novel peptide possesses great potential as an antimicrobial agent.

Keywords

References

  1. Fontana R, Mendes MA, de Souza BM, Konno K, Cesar LM, Malaspina O, et al. 2004. Jelleines: a family of antimicrobial peptides from the Royal Jelly of honybees (Apis mellifera). Peptides 2: 919-928.
  2. Hoffman JA, Kafatos FC, Janeway CA, Ezekowitz RA. 1999. Phylogenetic perspectives in innate immunity. Science 284: 1313-1318. https://doi.org/10.1126/science.284.5418.1313
  3. Hwang B, Hwang, JS, Lee J, Kim JK, Kim SR, Kim Y, et al. 2011. Induction of yeast apoptosis by an antimicrobial peptide, Papiliocin. Biochem. Biophys. Res. Commun. 408: 89-93. https://doi.org/10.1016/j.bbrc.2011.03.125
  4. Hwang JS, Lee J, Hwang B, Nam SH, Yun EY, Kim SR, et al. 2010. Isolation and characterization of Psacotheasin, a novel Knottin-type antimicrobial peptide, from Psacothea hilaris. J. Microbiol Biotechnol. 20: 708-711. https://doi.org/10.4014/jmb.1002.02003
  5. Kim SR, Hong MY, Park SW, Choi KH, Yun EY, Goo TW, et al. 2010. Characterization and cDNA cloning of a cecropin-like antimicrobial peptide, papiliocin, from the swallowtail butterfly, Papilio Xuthus. Mol. Cells 29: 419-423. https://doi.org/10.1007/s10059-010-0050-y
  6. Kim J, Jacob B, Jang M, Kwak C, Lee Y, Son K, et al. 2019. Development of a novel Short 12-meric papiliocin-derived peptide that is effective against gram-negative sepsis. Sci. Rep. 7: 3817. https://doi.org/10.1038/s41598-017-04201-x
  7. Klepserv ME, Malone D, Lewis RE, Ernst EJ, Pfaller MA. 2000. Evaluation of voriconazole pharmacodynamics using time-kill methodology. Antimicrob. Agents Chemother. 44: 1917-1920. https://doi.org/10.1128/AAC.44.7.1917-1920.2000
  8. Lee J, Hwang JS, Hwang B, Kim JK, Kim SR, Kim Y, et al. 2010. Membrane perturbation induced by papiliocin peptide, derived from Papilio xuthus, in Candida albicans. J. Microbiol. Biotechnol. 20: 1185-1188. https://doi.org/10.4014/jmb.1004.04014
  9. Lei J, Sun L, Huang S, Zhu C, Li P, He J, et al. 2019. The antimicrobial peptides and their potential clinical applications. Am. J. Trans. Res. 11: 3919-3931.
  10. Leontiadou H, Mark AE, Marrink SJ. 2006. Antimicrobial peptides in action. J. Am. Chem. Soc. 128: 12156-12161. https://doi.org/10.1021/ja062927q
  11. Melo MN, Ferre R, Castanho MA. 2009. Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations. Nat. Rev. Microbiol. 7: 245-250. https://doi.org/10.1038/nrmicro2095
  12. Nikaido H. 2010. Multidrug resistance in bacteria. Annu. Rev. Biochem. 78: 119-146. https://doi.org/10.1146/annurev.biochem.78.082907.145923
  13. Pushpanathan M, Gunasekaran P, Rajendhran J. 2013. Antimicrobial peptides: versatile biological properties. Int. J. Pept. 2013: 675391.
  14. Qi X, Zhou C, Li P, Xu W, Cao Y, Ling H, et al. 2010. Novel short antibacterial and antifungal peptides with low cytotoxicity: efficacy and action mechanisms. Biochem. Biophys. Res. Commun. 398: 594-600. https://doi.org/10.1016/j.bbrc.2010.06.131
  15. Raguse TL, Porter EA, Weisblum B, Gellman SH. 2002. Structure-activity studies of 14-helical antimicrobial beta-peptides: probing the relationship between conformational stability and antimicrobial potency. J. Am. Chem. Soc. 124: 12774-12785. https://doi.org/10.1021/ja0270423
  16. Rathinakumar R, Wimley WC. 2008. Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes. J. Am. Chem. Soc. 130: 9849-9858. https://doi.org/10.1021/ja8017863
  17. Son K, Kim J, Jang M, Chauhan AK, Kim Y. 2019. Effects of C-terminal residues of 12-mer peptides on antibacterial efficacy and mechanism. J. Microbiol. Biotechnol. 29: 1707-1716. https://doi.org/10.4014/jmb.1907.07061
  18. Zelezetsky I, Tossi A. 2006. Alpha-helical antimicrobial peptides-using a sequence template to guide structure-activity relationship studies. Biochim. Biophys. Acta 1758: 1436-1449. https://doi.org/10.1016/j.bbamem.2006.03.021
  19. Zhang L, Gallo RL. 2016. Antimicrobial peptides. Curr. Biol. 26: R14-R19. https://doi.org/10.1016/j.cub.2015.11.017

Cited by

  1. Butterfly Conservation in China: From Science to Action vol.11, pp.10, 2020, https://doi.org/10.3390/insects11100661