Abstract
Two lipopeptide antibiotics, pelgipeptins C and D, were isolated from Paenibacillus elgii B69 strain. The molecular masses of the two compounds were both determined to be 1,086 Da. Mass-spectrometry, amino acid analysis and NMR spectroscopy indicated that pelgipeptin C was the same compound as BMY-28160, while pelgipeptin D was identified as a new antibiotic of the polypeptin family. These two peptides were active against all the tested microorganisms, including antibiotic-resistant pathogenic bacterial strains such as methicillin-resistant Staphylococcus aureus (MRSA). Time-kill assays demonstrated that pelgipeptin D exhibited rapid and effective bactericidal action against MRSA at 4×MIC. Based on acute toxicity test, the intraperitoneal LD50 value of pelgipeptin D was slightly higher than that of the structurally related antimicrobial agent polymyxin B. Pelgipeptins are highly potent antibacterial and antifungal agents, particularly against MRSA, and warrant further investigation as possible therapeutic agents for bacteria infections resistant to currently available antibiotics.
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Araújo da Silva, K., J. Salles, L. Seldin, and J. van Elsas. 2003. Application of a novel Paenibacillus-specific PCR-DGGE method and sequence analysis to assess the diversity of Paenibacillus spp. In the maize rhizosphere. J. Microbiol. Methods 54, 213–231.
Ash, C., F. Priest, and M. Collins. 1993. Molecular identification of rRNA group 3 Bacilli (ash, farrow, wallbanks and collins) using a PCR probe test. Antonie van Leeuwenhoek. 64, 253–260.
Chen, L., N. Wang, X. Wang, J. Hu, and S. Wang. 2010. Characterization of two anti-fungal lipopeptides produced by Bacillus amyloliquefaciens SH-B10. Bioresour. Technol. 101, 8822–8827.
Choi, S.K., S.Y. Park, R. Kim, S.B. Kim, C.H. Lee, J.F. Kim, and S.H. Park. 2009. Identification of a polymyxin synthetase gene cluster of Paenibacillus polymyxa and heterologous expression of the gene in Bacillus subtilis. J. Bacteriol. 191, 3350–3358.
Fujii, K., K. Sivonen, T. Kashiwagi, K. Hirayama, and K. Harada. 1999. Nostophycin, a novel cyclic peptide from the toxic Cyanobacterium nostoc sp. 152. J. Org. Chem. 64, 5777–5782.
Gangolli, S.D., P. Simson, M.T. Lis, B. Cheng, R.F. Crampton, and D.M. Matthews. 1970. Amino acid and peptide uptake in protein absorption. Clin. Sci. 39, 18.
Kim, P.I., H. Bai, D. Bai, H. Chae, S. Chung, Y. Kim, R. Park, and et al. 2004. Purification and characterization of a lipopeptide produced by Bacillus thuringiensis CMB26. J. Appl. Microbiol. 97, 942–949.
Kim, P.I., J. Ryu, Y. Kim, and Y. Chi. 2010. Production of biosurfactant lipopeptides iturin a, fengycin, and surfactin a from Bacillus subtilis CMB32 for control of colletotrichum gloeosporioides. J. Microbiol. Biotechnol. 20, 138–145.
Klevens, R.M., M.A. Morrison, J. Nadle, S. Petit, K. Gershman, S. Ray, L.H. Harrison, and et al. 2007. Invasive methicillin-resistant Staphylococcus aureus infections in the united states. JAMA. 298, 1763–1771.
Levine, D. 2006. Vancomycin: A history. Clin. Infect. Dis. 42, S5–12.
Li, J., P.K. Beatty, S. Shah, and S.E. Jensen. 2007. Use of PCR-targeted mutagenesis to disrupt production of fusaricidin-type antifungal antibiotics in Paenibacillus polymyxa. Appl. Environ. Microbiol. 73, 3480–3489.
McKay, G.A., S. Beaulieu, F.F. Arhin, A. Belley, I. Sarmiento Jr, and G. Moeck. 2009. Time-kill kinetics of oritavancin and comparator agents against Staphylococcus aureus, Eenterococcus faecalis and Enterococcus faecium. J. Antimicrob. Chemother. 63, 1191–1199.
McVay, C.S. and R.D. Rolfe. 2000. In vitro and in vivo activities of nitazoxanide against Clostridium difficile. Antimicrob. Agents Chemother. 44, 2254–2258.
Moellering, R. Jr. 2006. Vancomycin: A 50-year reassessment. Clin. Infect Dis. 42, S3–4.
Muto, C., J. Jernigan, B. Ostrowsky, H. Richet, W. Jarvis, J. Boyce, and B. Farr. 2003. Shea guideline for preventing nosocomial transmission of multidrug-resistant strains of Staphylococcus aureus and Enterococcus. Infect. Cont. Hosp. Ep. 24, 362–386.
Pirri, G., A. Giuliani, S. Nicoletto, L. Pizzuto, and A. Rinaldi. 2009. Lipopeptides as anti-infectives: A practical perspective. Cent. Eur. J. Biol. 4, 258–273.
Sogn, J.A. 1976. Structure of the peptide antibiotic polypeptin. J. Med. Chem. 19, 1228–1231.
Storm, D.R., K.S. Rosenthal, and P.E. Swanson. 1977. Polymyxin and related peptide antibiotics. Annu. Rev. Biochem. 46, 723–763.
Sugawara, K., M. Konishi, and H. Kawaguchi. 1984. BMY-28160, a new peptide antibiotic. J. Antibiot. 37, 1257–1259.
Takeuchi, Y., A. Murai, Y. Takahara, and M. Kainosho. 1979. The structure of permetin a, a new polypeptin type antibiotic produced by Bacillus circulans. J. Antibiot. 32, 121–129.
Thiericke, R. and J. Rohr. 1993. Biological variation of microbial metabolites by precursor-directed biosynthesis. Nat. Prod. Rep. 10, 265–289.
Wang, Z. and X. Liu. 2008. Medium optimization for antifungal active substances production from a newly isolated Paenibacillus sp. Using response surface methodology. Bioresour. Technol. 99, 8245–8251.
Weigel, L., D. Clewell, S. Gill, N. Clark, L. McDougal, S. Flannagan, J. Kolonay, and et al. 2003. Genetic analysis of a high-level vancomycin-resistant isolate of Staphylococcus aureus. Science 302, 1569.
Wu, X.C., X.B. Shen, R. Ding, C.D. Qian, H.H. Fang, and O. Li. 2010. Isolation and partial characterization of antibiotics produced by Paenibacillus elgii B69. FEMS Microbiol. Lett. 320, 32–38.
Wu, X.C., C.D. Qian, H.H. Fang, Y.P. Wen, J.Y. Zhou, Z.J. Zhan, R. Ding, and et al. 2011. Paenimacrolidin, a novel macrolide antibiotic from Paenibacillus sp. F6-b70 active against methicillin-resistant Staphylococcus aureus. Microb. Biotechnol. 4, 491–502.
Zhao, Z.H., Y.B. Ma, C. Dai, R.M. Zhao, S.R. Li, Y.L. Wu, Z.J. Cao, and W.X. Li. 2009. Imcroporin, a new cationic antimicrobial peptide from the venom of the scorpion Isometrus maculates. Antimicrob. Agents Chemother. 53, 3472–3477.
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Ding, R., Wu, XC., Qian, CD. et al. Isolation and identification of lipopeptide antibiotics from Paenibacillus elgii B69 with inhibitory activity against methicillin-resistant Staphylococcus aureus . J Microbiol. 49, 942–949 (2011). https://doi.org/10.1007/s12275-011-1153-7
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DOI: https://doi.org/10.1007/s12275-011-1153-7