Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Antimicrobial Activity of the Synthetic Peptide Scolopendrasin II from the Centipede Scolopendra subspinipes mutilans

  • Kwon, Young-Nam (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Lee, Joon Ha (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Kim, In-Woo (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Kim, Sang-Hee (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Yun, Eun-Young (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Nam, Sung-Hee (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Ahn, Mi-Young (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Jeong, MiHye (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Kang, Dong-Chul (Ilsong Institute of Life Science, Hallym University) ;
  • Lee, In Hee (Department of Biotechnology, Hoseo University) ;
  • Hwang, Jae Sam (Department of Agricultural Biology, National Academy of Agricultural Science, RDA)
  • Received : 2013.06.07
  • Accepted : 2013.06.26
  • Published : 2013.10.28
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Abstract

The centipede Scolopendra subpinipes mutilans is a medicinally important arthropod species. However, its transcriptome is not currently available and transcriptome analysis would be useful in providing insight into a molecular level approach. Hence, we performed de novo RNA sequencing of S. subpinipes mutilans using next-generation sequencing. We generated a novel peptide (scolopendrasin II) based on a SVM algorithm, and biochemically evaluated the in vitro antimicrobial activity of scolopendrasin II against various microbes. Scolopendrasin II showed antibacterial activities against gram-positive and -negative bacterial strains, including the yeast Candida albicans and antibiotic-resistant gram-negative bacteria, as determined by a radial diffusion assay and colony count assay without hemolytic activity. In addition, we confirmed that scolopendrasin II bound to the surface of bacteria through a specific interaction with lipoteichoic acid and a lipopolysaccharide, which was one of the bacterial cell-wall components. In conclusion, our results suggest that scolopendrasin II may be useful for developing peptide antibiotics.

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References

  1. Adis J, Harvey MS. 2000. How many Arachnida and Myriapoda are there world-wide and in Amazonia? Stud. Neotrop. Fauna Environ. 35: 139-141.
  2. Baldridge GD, Kurtti TJ, Munderloh UG. 2005. Susceptibility of Rickettsia monacensis and Rickettsia peacockii to Cecropin A, Ceratotoxin A, and lysozyme. Curr. Microbiol. 51: 233-238. https://doi.org/10.1007/s00284-005-4532-7
  3. Brahmachary M, Krishnan SP, Koh JL, Khan AM, Seah SH, Tan TW, et al. 2004. ANTIMIC: a database of antimicrobial sequences. Nucleic Acids Res. 32: D586-D589. https://doi.org/10.1093/nar/gkh032
  4. Bulet P, Stocklin R. 2005. Insect antimicrobial peptides: structures, properties and gene regulation. Protein Pept. Lett. 12: 3-11. https://doi.org/10.2174/0929866053406011
  5. Conlon JM. 2011. The contribution of skin antimicrobial peptides to the system of innate immunity in anurans. Cell Tissue Res. 343: 201-212. https://doi.org/10.1007/s00441-010-1014-4
  6. Devine DA, Hancock RE. 2002. Cationic peptides: distribution and mechanisms of resistance. Curr. Pharm. Des. 8: 703-714. https://doi.org/10.2174/1381612023395501
  7. Garnier J, Gibrat JF, Robson B. 1996. GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol. 266: 540-553. https://doi.org/10.1016/S0076-6879(96)66034-0
  8. Hancock RE, Chapple DS. 1999. Peptide antibiotics. Antimicrob. Agents Chemother. 43: 1317-1323.
  9. Hwang JS, Lee J, Kim YJ, Bang HS, Yun EY, Kim SR, et al. 2009. Isolation and characterization of a defensin-like peptide (Coprisin) from the dung beetle, Copris tripartitus. Int. J. Pept. doi: 10.1155/2009/136284.
  10. Hwang PM, Vogel HJ. 1998. Structure-function relationships of antimicrobial peptides. Biochem. Cell Biol. 76: 235-246. https://doi.org/10.1139/o98-026
  11. Jenssen H, Hamill P, Hancock RE. 2006. Peptide antimicrobial agents. Clin. Microbiol. Rev. 19: 491-511. https://doi.org/10.1128/CMR.00056-05
  12. Mendes MA, de Souza BM, Palma MS. 2005. Structural and biological characterization of three novel mastoparan peptides from the venom of the neotropical social wasp Protopolybia exigua (Saussure). Toxicon 45: 101-106. https://doi.org/10.1016/j.toxicon.2004.09.015
  13. Pasupuleti M, Schmidtchen A, Malmsten M. 2012. Antimicrobial peptides: key components of the innate immune system. Crit. Rev. Biotechnol. 32: 143-171. https://doi.org/10.3109/07388551.2011.594423
  14. Pemberton RW. 1999. Insects and other arthropods used as drugs in Korean traditional medicine. J. Ethnopharmacol. 65: 207-216. https://doi.org/10.1016/S0378-8741(98)00209-8
  15. Peng K, Kong Y, Zhai L, Wu X, Jia P, Liu J, et al. 2010. Two novel antimicrobial peptides from centipede venoms. Toxicon 55: 274-279. https://doi.org/10.1016/j.toxicon.2009.07.040
  16. Scott MG, Hancock RE. 2000. Cationic antimicrobial peptides and their multifunctional role in the immune system. Crit. Rev. Immunol. 20: 407-431.
  17. Seshadri Sundararajan V, Gabere MN, Pretorius A, Adam S, Christoffels A, Lehvaslaiho M, et al. 2012. DAMPD: a manually curated antimicrobial peptide database. Nucleic Acids Res. 40: D1108-D1112. https://doi.org/10.1093/nar/gkr1063
  18. Smolowitz R. 2013. A review of current state of knowledge concerning Perkinsus marinus effects on Crassostrea virginica (Gmelin) (the eastern oyster). Vet. Pathol. 50: 404-411. https://doi.org/10.1177/0300985813480806
  19. Steinberg DA, Lehrer RI. 1997. Designer assays for antimicrobial peptides. Methods Mol. Biol. 78: 169-186.
  20. Wenhua R, Shuangquan Z, Daxiang S, Kaiya Z, Guang Y. 2006. Induction, purification and characterization of an antibacterial peptide scolopendrin I from the venom of centipede Scolopendra subspinipes mutilans. Indian J. Biochem. Biophys. 43: 88-93.

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