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Biochemistry Research International
Volume 2016 (2016), Article ID 1091290, 5 pages
http://dx.doi.org/10.1155/2016/1091290
Research Article

Contribution of Cell Surface Hydrophobicity in the Resistance of Staphylococcus aureus against Antimicrobial Agents

1Animal Biochemistry Division, National Dairy Research Institute, Karnal, Haryana 132001, India
2Animal Biotechnology Division, National Dairy Research Institute, Karnal, Haryana 132001, India
3Dairy Cattle Nutrition Division, National Dairy Research Institute, Karnal, Haryana 132001, India

Received 9 September 2015; Revised 19 November 2015; Accepted 11 January 2016

Academic Editor: Tzi B. Ng

Copyright © 2016 Puja Lather et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. G. Kenny, D. Ward, E. Josefsson et al., “The Staphylococcus aureus response to unsaturated long chain free fatty acids: survival mechanisms and virulence implications,” PLoS ONE, vol. 4, no. 2, Article ID e4344, 2009. View at Publisher · View at Google Scholar · View at Scopus
  2. M. K. Sandel and J. L. McKillip, “Virulence and recovery of Staphylococcus aureus relevant to the food industry using improvements on traditional approaches,” Food Control, vol. 15, no. 1, pp. 5–10, 2004. View at Publisher · View at Google Scholar · View at Scopus
  3. A. G. Mainous and C. Pomeroy, Management of Antimicrobials in Infectious Diseases, Humana Press, 2001. View at Publisher · View at Google Scholar
  4. H. G. Boman, “Peptide antibiotics and their role in innate immunity,” Annual Review of Immunology, vol. 13, pp. 61–92, 1995. View at Publisher · View at Google Scholar · View at Scopus
  5. M. Zasloff, “Antimicrobial peptides of multicellular organisms,” Nature, vol. 415, no. 6870, pp. 389–395, 2002. View at Publisher · View at Google Scholar · View at Scopus
  6. E. Martin, T. Ganz, and R. I. Lehrer, “Defensins and other endogenous peptide antibiotics of vertebrates,” Journal of Leukocyte Biology, vol. 58, no. 2, pp. 128–136, 1995. View at Google Scholar · View at Scopus
  7. R. E. W. Hancock and H.-G. Sahl, “Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies,” Nature Biotechnology, vol. 24, no. 12, pp. 1551–1557, 2006. View at Publisher · View at Google Scholar · View at Scopus
  8. D. M. Ojcius and J. D.-E. Young, “Cytolytic pore forming proteins and peptides, is there a common structural motif?” Trends in Biochemical Sciences, vol. 16, no. 1, pp. 225–229, 1991. View at Publisher · View at Google Scholar · View at Scopus
  9. H. G. Sahl, “Pore formation in bacterial membranes by cationic lantibiotics,” in Nisin and Novel Lantibiotics, G. Jung and H. G. Sahl, Eds., pp. 347–358, ESCOM Science, Leiden, The Netherlands, 1991. View at Google Scholar
  10. I. F. Nes and H. Holo, “Class II antimicrobial peptides from lactic acid bacteria,” Biopolymers, vol. 55, no. 1, pp. 50–61, 2000. View at Publisher · View at Google Scholar · View at Scopus
  11. T. R. Klaenhammer, “Genetics of bacteriocins produced by lactic acid bacteria,” FEMS Microbiology Reviews, vol. 12, no. 1–3, pp. 39–86, 1993. View at Publisher · View at Google Scholar · View at Scopus
  12. H. S. Thippeswamy, S. K. Sood, R. Venkateswarlu, and I. Raj, “Membranes of five-fold alamethicin-resistant Staphylococcus aureus, Enterococcus faecalis and Bacillus cereus show decreased interactions with alamethicin due to changes in membrane fluidity and surface charge,” Annals of Microbiology, vol. 59, no. 3, pp. 593–601, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. K. R. Foster, “Hamiltonian medicine: why the social lives of pathogens matter,” Science, vol. 308, no. 5726, pp. 1269–1270, 2005. View at Publisher · View at Google Scholar · View at Scopus
  14. A. Peschel and H.-G. Sahl, “The co-evolution of host cationic antimicrobial peptides and microbial resistance,” Nature Reviews Microbiology, vol. 4, no. 7, pp. 529–536, 2006. View at Publisher · View at Google Scholar · View at Scopus
  15. J. Mehla and S. K. Sood, “Substantiation in Enterococcus faecalis of dose-dependent resistance and cross-resistance to pore-forming antimicrobial peptides by use of a polydiacetylene-based colorimetric assay,” Applied and Environmental Microbiology, vol. 77, no. 3, pp. 786–793, 2011. View at Publisher · View at Google Scholar · View at Scopus
  16. C.-W. Wu, L.-J. Yin, and S.-T. Jiang, “Purification and characterization of bacteriocin form Pediococcus pentosaceus ACCEL,” Journal of Agricultural and Food Chemistry, vol. 52, no. 5, pp. 1146–1151, 2004. View at Publisher · View at Google Scholar · View at Scopus
  17. J. D. Marugg, C. F. Gonzalez, B. S. Kunka et al., “Cloning, expression, and nucleotide sequence of genes involved in production of pediocin PA-1, and bacteriocin from Pediococcus acidilactici PAC 1.0,” Applied and Environmental Microbiology, vol. 58, no. 8, pp. 2360–2367, 1992. View at Google Scholar
  18. R. Yang, M. C. Johnson, and B. Ray, “Novel method to extract large amounts of bacteriocins from lactic acid bacteria,” Applied and Environmental Microbiology, vol. 58, no. 10, pp. 3355–3359, 1992. View at Google Scholar · View at Scopus
  19. P. Lather, A. K. Mohanty, P. Jha, A. K. Garsa, and S. K. Sood, “Changes associated with cell membrane composition of Staphylococcus aureus on acquisition of resistance against class IIa bacteriocin and its in vitro substantiation,” European Food Research and Technology, vol. 240, no. 1, pp. 101–107, 2014. View at Publisher · View at Google Scholar · View at Scopus
  20. F. Reifsteck, S. Wee, and B. J. Wilkinson, “Hydrophobicity-hydrophilicity of Staphylococci,” Journal of Medical Microbiology, vol. 24, no. 1, pp. 65–73, 1987. View at Publisher · View at Google Scholar · View at Scopus
  21. L. H. Deegan, P. D. Cotter, C. Hill, and P. Ross, “Bacteriocins: biological tools for bio-preservation and shelf-life extension,” International Dairy Journal, vol. 16, no. 9, pp. 1058–1071, 2006. View at Publisher · View at Google Scholar · View at Scopus
  22. M. B. Hanlin and N. Kalchayanand, “Bacteriocins of lactic acid bacteria in combination have greater antibacterial activity,” Journal of Food Protection, vol. 56, no. 3, pp. 252–255, 1993. View at Google Scholar
  23. X. Ming and M. A. Daeschel, “Correlation of cellular phospholipid content with nisin resistance of Listeria monocytogenes Scott A,” Journal of Food Protection, vol. 58, no. 4, pp. 416–420, 1995. View at Google Scholar · View at Scopus
  24. R. I. Lehrer and T. Ganz, “Defensins of vertebrate animals,” Current Opinion in Immunology, vol. 14, no. 1, pp. 96–102, 2002. View at Publisher · View at Google Scholar · View at Scopus
  25. H. Jenssen, T. J. Gutteberg, and T. Lejon, “Modelling the anti-herpes simplex virus activity of small cationic peptides using amino acid descriptors,” Journal of Peptide Research, vol. 66, no. 1, pp. 48–56, 2006. View at Publisher · View at Google Scholar · View at Scopus
  26. A. S. Bayer, R. Prasad, J. Chandra et al., “In vitro resistance of Staphylococcus aureus to thrombin-induced platelet microbicidal protein is associated with alterations in cytoplasmic membrane fluidity,” Infection and Immunity, vol. 68, no. 6, pp. 3548–3553, 2000. View at Publisher · View at Google Scholar · View at Scopus
  27. A. Peschel and L. Vincent Collins, “Staphylococcal resistance to antimicrobial peptides of mammalian and bacterial origin,” Peptides, vol. 22, no. 10, pp. 1651–1659, 2001. View at Publisher · View at Google Scholar · View at Scopus
  28. L. M. Cintas, J. M. Rodriguez, M. F. Fernandez et al., “Isolation and characterization of pediocin L50, a new bacteriocin from Pediococcus acidilactici with a broad inhibitory spectrum,” Applied and Environmental Microbiology, vol. 61, no. 7, pp. 2643–2648, 1995. View at Google Scholar · View at Scopus
  29. A. Gravesen, K. Sørensen, F. M. Aarestrup, and S. Knøchel, “Spontaneous nisin-resistant Listeria monocytogenes mutants with increased expression of a putative penicillin-binding protein and their sensitivity to various antibiotics,” Microbial Drug Resistance, vol. 7, no. 2, pp. 127–135, 2001. View at Publisher · View at Google Scholar · View at Scopus
  30. M. Rosenberg, D. Gutnick, and E. Rosenberg, “Adherence of bacteria to hydrocarbons: a simple method for measuring cell-surface hydrophobicity,” FEMS Microbiology Letters, vol. 9, no. 1, pp. 29–33, 1980. View at Publisher · View at Google Scholar · View at Scopus
  31. C. M. Waters and G. M. Dunny, “Analysis of functional domains of the Enterococcus faecalis pheromone-induced surface protein aggregation substance,” Journal of Bacteriology, vol. 183, no. 19, pp. 5659–5667, 2001. View at Publisher · View at Google Scholar · View at Scopus
  32. R. Kumariya, S. K. Sood, Y. S. Rajput, and A. K. Garsa, “Gradual pediocin PA-1 resistance in Enterococcus faecalis confers cross-protection to diverse pore-forming cationic antimicrobial peptides displaying changes in cell wall and mannose PTS expression,” Annals of Microbiology, vol. 65, no. 2, pp. 721–732, 2014. View at Publisher · View at Google Scholar · View at Scopus
  33. S. R. Clarke, R. Mohamed, L. Bian et al., “The Staphylococcus aureus surface protein IsdA mediates resistance to innate defenses of human skin,” Cell Host and Microbe, vol. 1, no. 3, pp. 199–212, 2007. View at Publisher · View at Google Scholar · View at Scopus
  34. F. C. Neuhaus and J. Baddiley, “A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria,” Microbiology and Molecular Biology Reviews, vol. 67, no. 4, pp. 686–723, 2003. View at Publisher · View at Google Scholar · View at Scopus
  35. D. Morisset, J.-M. Berjeaud, D. Marion, C. Lacombe, and J. Frère, “Mutational analysis of mesentericin Y105, an anti-Listeria bacteriocin, for determination of impact on bactericidal activity, in vitro secondary structure, and membrane interaction,” Applied and Environmental Microbiology, vol. 70, no. 8, pp. 4672–4680, 2004. View at Publisher · View at Google Scholar
  36. J. M. Yarwood and P. M. Schlievert, “Quorum sensing in Staphylococcus infections,” Journal of Clinical Investigation, vol. 112, no. 11, pp. 1620–1625, 2003. View at Publisher · View at Google Scholar · View at Scopus
  37. M. Dufour, J. M. Manson, P. J. Bremer, J.-P. Dufour, G. M. Cook, and R. S. Simmonds, “Characterization of monolaurin resistance in Enterococcus faecalis,” Applied and Environmental Microbiology, vol. 73, no. 17, pp. 5507–5515, 2007. View at Publisher · View at Google Scholar · View at Scopus
  38. M. Rosenberg and R. J. Doyle, “Microbial cell surface hydrophobicity: history, measurement, and significance,” in Microbial Cell Surface Hydrophobicity, R. J. Doyle and M. Rosenberg, Eds., pp. 1–37, American Society for Microbiology, Washington, DC, USA, 1990. View at Google Scholar