Effects of an Antimicrobial Substance from Bombycis corpus on Antibiotic Resistant Microbes

백강잠으로부터 분리한 항균물질의 항생제 내성균에 대한 효과

  • Lee, Hyeon-Woo (Department of Biochemistry, Yonsei University Wonju College of Medicine, Eurim Biotec Co.) ;
  • Um, Jeong-Sun (Department of Oriental Medical Food & Nutrition, Semyung University) ;
  • Ko, Mi-Kyung (Department of Oriental Medical Food & Nutrition, Semyung University) ;
  • Kim, Mi-Kyung (Department of Oriental Medical Food & Nutrition, Semyung University) ;
  • Eun, Jae-Soon (College of Pharmacy, Woosuk University) ;
  • Jeon, Hoon (College of Pharmacy, Woosuk University) ;
  • Leem, Jae-Yoon (Department of Oriental Medical Food & Nutrition, Semyung University, College of Pharmacy, Woosuk University)
  • 이현우 (연세대학교 원주의과대학, 의림 바이오텍) ;
  • 엄정선 (세명대학교 한방식품영양학과) ;
  • 고미경 (세명대학교 한방식품영양학과) ;
  • 김미성 (세명대학교 한방식품영양학과) ;
  • 은재순 (우석대학교 약학대학) ;
  • 전훈 (우석대학교 약학대학) ;
  • 임재윤 (세명대학교 한방식품영양학과, 우석대학교 약학대학)
  • Published : 2007.08.31

Abstract

Bombycis corpus, a batryticated silkworm and white-stiff silkworm, is an oriental drug consisting of the dried larva of silkworm, dead and stiffened due to the infection of Beauveria. An peptidyl antimicrobial molecule was purified from B. corpus by reverse phase-column chromatography and HPLC. Its molecular weight was determined to be 2295.45 by using matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry. Its antimicrobial activity was diminished by trypsin digestion. It exhibited a broad antimicrobial spectrum against not only Gram-negative, but also Gram- positive bacteria. Furthermore, it was found to have an antimicrobial activity against vancomycin-resistant enterococci (VRE), methicillin-resistant S. arureus (MRSA), and vancomycin-intermediate resistant S. arureus (VISA). It may be a useful molecule for a new antibiotic development, especially against antibiotic resistant microbe. This substance may play a role in the defense system of this animal against Beauveria bassiana. This is the first report of a peptidyl antimicrobial substance from B. corpus.

Keywords

References

  1. Schroder, J. M. and Harder, J. : Antimicrobial skin peptides and proteins. Cell. Mol. Life Sci. 63, 469 (2006) https://doi.org/10.1007/s00018-005-5364-0
  2. Andreu, D. and Rivas, L. : Animal antimicrobial peptide: An overview. Biopolymers 55, 415 (1998)
  3. Matsuyama, K. and Natori, S. : Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina. J. BioI. Chem. 263, 17112 (1988)
  4. Boman, H. G., Nilsson, I. and Rasmuson, B. : Inducible antibacterial defence system in Drosophila. Nature 237, 232 (1972)
  5. Leem, J.-Y., Nishimura, C., Kurata, S., Shimada, I., Kobayashi, A. and Natori, S. : Purification and characterization of N-${\beta}$-alanyl-5-S-glutathionyl-3,4-dihydroxyphenylalanine, a novel antibacterial substance of Sarcophaga peregrina (flesh fly). J. BioI. Chem. 271, 13573 (1996)
  6. Nakajima, Y., Alvarez-Bravo, J., Cho, J., Homma, K., Kanegasaki, S. and Natori, S. : Chemotherapeutic activity of synthetic antimicrobial peptides: correlation between chemotherapeutic activity and neutrophil-activating activity. FEBS Lett. 415, 64 (1997)
  7. Zasloff, M. : Antimicrobial peptides of multicellular organisms. Nature 415, 389 (2002)
  8. Wilson, C. and Peter, F. M. : Biodiversity. Natl. Acad. Press (1988)
  9. Hoffmann, J. A., Janeway, C. A. Jr. and Natori, S. : Phylogenetic perspectives in immunity-The insect host defense. Molecular Biology Intelligence Unit., R.G. Landes Co. (1994)
  10. Pharmacopoeia Commission of the Ministry of Public Health, P.R. China : A coloured atlas of the Chinese materia medica specified in pharmacopoeia of the people's republic of China, Guangdong science & technology press, p. 482 (1995)
  11. Hiramatsu, K., Cui, L., Kuroda, M. and Ito, T. : The emergence and evolution of methicillin-resistant Staphylococcus aureus. Trends of Microbiol. 9, 486 (2001)
  12. Baba, T., Takeuchi, F., Kuroda, M., Yuzawa, H., Aoki, K., Oguchi, A., Nagai, Y., Iwama, N., Asano, K., Naimi, T., Kuroda, H., Cui, Li., Yamamoto, K. and Hiramatsu, K. : Genome and virulence determinants of high virulence community-acquired MRSA. Lancet 359, 1819 (2002)
  13. Kim, M. N., Pai, C. H., Woo, J. H., Ryu, J. S. and Hiramatsu, K. : Vancomycin-intermediate Staphylococcus aureus in Korea. J. Clin. Microbiol. 38, 3879 (2000)
  14. Arthur, M., Reynolds, P. and Courvalin, P. : Glycopeptide resistance in enterococci. Trends Microbiol. 4, 401 (1996)
  15. NCCLS. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically. NCCLS approved standard M7-A6. NCCLS, Wayne, Pa. (2003)
  16. Marchese, A., Debbia, E. A., Tonoli, E., Gualco, L. and Schito, A. M. : In vitro activity of thiamphenicol against multiresistant Streptococcus pneumoniae, Haemophilus influenzae and Staphylococcus aureus in Italy. J. Chemother. 14, 554 (2002)
  17. Linares, J. : The VISA/GISA problem: therapeutic implications, Clin. Microbiol. Infect. 7, 815 (2001)
  18. Chang, S., Sievert, D. M., Hageman, J. C., Boulton, M. L., Tenover, F. C., Downes, F. P., Shah, S., Rudrik, J. T., Pupp, G. R., Brown, W.J., Cardo, D. and Fridkin, S. K. : Infection with vancomycin-resistant Staphylococcus aureus containing the vanA resistance gene. N. Engl. J. Med. 384, 1342 (2003)
  19. Tsiodras, S., Gold, H. S., Sakoulas, G., Eliopoulos, G. M., Wennersten, C., Venkataraman, L., Moellering, R. C. and Ferraro, M. J. : Linezolid resistance in a clinical isolate of Staphylococcus aureus. Lancet 358, 207 (2001) https://doi.org/10.1016/S0140-6736(00)05272-7
  20. Brogden, K. A. : Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3, 238 (2005) https://doi.org/10.1038/nrmicro1098
  21. Mygind, P. H., Fischer, R. L., Schnorr, K. M., Hansen, M. T., Sonksen, C. P., Ludvigsen, S., Raventos, D., Buskov, S., Christensen, B., De Maria, L., Taboureau, O., Yaver, D., Elvig-Jorgensen, S. G., Sorensen, M. V., Christensen, B. E., Kjaerulff, S., Frimodt-Moller, N., Lehrer, R. I., Zasloff, M. and Kristensen, H. H. : Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus. Nature 437, 975 (2005) https://doi.org/10.1038/nature04051