Distribution of O-Acetylation in the Peptidoglycan from Proteus mirabilis 19

  • Anthony J. Clarke
  • Steve Gyorffy
  • James W. Chase
Part of the Federation of European Microbiological Societies Symposium Series book series (FEMS, volume 65)

Abstract

The detection of O-acetylated peptidoglycan has previously required the isolation and purification of peptidoglycan from the study microorganisms followed by the release (saponification) and quantitation of acetate. Since this methodology is laborious and in addition, the ester-linked acetyl moiety is highly labile, it is not surprising that the prevalence of O-acetylated peptidoglycan among the eubacteria is largely unknown. The only microorganisms confirmed to possess O-acetylated peptidoglycan include Lactobacillus fermentum, Moraxella glucidolytica, Neisseria gonorrhoeae, N. perflava, Proteus mirabilis, P. vulgaris, Pseudomonas alcaligenes, Staphylococcus aureus and Streptococcus faecalis (reviewed in Clarke and Dupont, 1992). Many of these microorganisms represent important human pathogens but a correlation, if any, between peptidoglycan O-acetylation and pathogenicity/ virulence has not been examined. Moreover, very little is known regarding both the physiological role and the mechanistic process of the modification (Clarke and Dupont, 1992).

Keywords

Immunoelectron Microscopy Neisseria Gonorrhoeae Proteus Mirabilis Immunogold Labelling Booster Immunization 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Blundell, J.K. and Perkins, H.R. (1985) Selectivity for O-acetylated peptidoglycan during endopeptidase action by permeabilized Neisseria gonorrhoeae. FEMS Microbiol. Lett. 30, 67–69.CrossRefGoogle Scholar
  2. Clarke, A.J. and Dupont, C. (1992) O-Acetylated peptidoglycan: its occurrence, pathobiological significance, and biosynthesis. Can J. Microbiol. In press.Google Scholar
  3. Dupont, C. and Clarke, A.J. (1991) Dependence of lysozyme-catalysed solubilization of Protues mirabilis peptidoglycan on the extent of O-acetylation. Eur. J. Biochem. 195, 763–769.PubMedCrossRefGoogle Scholar
  4. Esser, A.F. (1991) Big MAC attack: complement proteins cause leaky patches. Immunol. Today 12, 316–318.PubMedCrossRefGoogle Scholar
  5. Gmeiner, J. and Sarnow, E. (1987) Murein biosynthesis in synchronized cells of Proteus mirabilis. Quantitative analysis of O-acetylated murein subunits and of chain terminators incorporated into the sacculus during the cell cycle. Eur. J. Biochem. 163, 389–395.PubMedCrossRefGoogle Scholar
  6. Heymer, J., Seidl, P. and Schleifer, K. (1985) Immunochemistry and biological activity of peptidoglycan, in “Immunology of the Bacterial Cell Envelope” (Stewart, D. and Davies, M., Eds.), pp. 11–46. John Wiley and Sons, New York.Google Scholar
  7. Hoyle, B.D. and Beveridge, T. (1983) Metal binding by the peptidoglycan sacculus of Escherichia coli K-12. Can. J. Microbiol. 30, 204–211.CrossRefGoogle Scholar
  8. Jackson, D.E., Wong, W., Swavely, T.S. and Shockman, G.D. (1983) Monoclonal antibodies that recognize bacterial cell wall peptidoglycan. Abstract No. K151. 83rd Annual Meeting of the American Society for Microbiology, March, New Orleans.Google Scholar
  9. Lam, J.S., MacDonald, L.A., Lam, M.Y.C., Duchesne, L.G.M. and Southam, G.S. (1987) Production and characterization of monoclonal antibodies against serotype strains of Pseudomonas aeruginosa. Infect. Immun. 55, 1051–1057.PubMedGoogle Scholar
  10. Oi, V.T. and Herzenberg, L.A. (1979) Immunoglobulin production hybrid cell lines, in “Selected Methods in Cellular Immunology” (Mishell, B.B. and Shiigi, S.M., Eds), pp. 351–371. W. H. Freeman & Co., San Francisco.Google Scholar
  11. Seidl, P.H. and Schleifer, K.H. (1985a) “Biological Properties of Peptidoglycan,” Walter de Gruyter, New York.Google Scholar
  12. Seidl, P.H. and Schleifer, K.H. (1985b) Structure and immunochemistry of peptidoglycan, in “Biological Properties of Peptidoglycan” (Seidl, P.H. and Schleifer, K.H. Eds.), pp. 1–20. Walter de Gruyter, New York.Google Scholar
  13. Timmell, T.E. (1964) Wood hemicelluloses: Part I. Adv. Carbohydr. Chem. 19, 247–302.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Anthony J. Clarke
    • 1
  • Steve Gyorffy
    • 1
  • James W. Chase
    • 1
  1. 1.Department of MicrobiologyUniversity of GuelphGuelphCanada

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