Hostname: page-component-586b7cd67f-2plfb Total loading time: 0 Render date: 2024-11-20T06:25:27.887Z Has data issue: false hasContentIssue false

Mechanisms of resistance of staphylococci grown in plasma to polymorph bactericidins

Published online by Cambridge University Press:  19 October 2009

Deboye O. Kolawole
Affiliation:
Department of Microbiology, University of Ife, Ile-Ife, Nigeria
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

The mechanisms whereby staphylococcal strains grown in plasma assume increased resistance to polymorph bactericidins were investigated. Observations reported here showed that cultural conditions could determine the path of conversion to resistance. Staphylococcal strains and mutants lacking either free coagulase or clumping factor or both all showed enhanced resistance after 10 h incubation in plasma proteins, thus giving no clear indication that these factors were involved in the interactions. In fact, prolonged incubation in bovine serum albumin (22 h) and ordinary broth medium (24 h) also resulted in increased resistance. A distinction between staphylococcal factors interacting specifically with plasma proteins and such non-specific conversions was obtained in two different ways. Stripping of a hypothetical surface protein by treatment with trypsin or 2 M potassium bromide rendered plasma- but not 24 h-broth organisms susceptible, indicating protein coating of plasma-grown organisms. Also free coagulase-positive strains and mutants incubated in plasma for 30 min were converted while those lacking both or possessing clumping factor alone were not. It therefore appears that one of the mechanisms of acquiring resistance involves a rapid interaction between staphylococcal-free coagulase and fibrinogen, resulting in the deposition of fibrin or fibrin derivatives on the bacterial surface.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1984

References

REFERENCES

Adlam, C., Pearce, J. H. & Smith, H. (1970). The interaction of staphylococci grown in in vivo and in vitro with polymorphonuclear leukocytes. Journal of Medical Microbiology 3, 157163.Google Scholar
Duthie, E. S. (1954). Evidence for two forms of staphylococcal coagulase. Journal of General Microbiology 10, 427436.Google Scholar
Ekstedt, R. D. & Bernhard, J. M. (1973). Preparation and characterization of a slime layer material produced by Staphylococcus aureus. Proceedings of the Society for Experimental Biology and Medicine 142, 8691.CrossRefGoogle ScholarPubMed
Forsgren, A. & Sjoquist, J. (1966). Protein A from Staphylococcus aureus. Journal of Immunology 97, 822827.CrossRefGoogle Scholar
Forsgren, A. & Sjoquist, J. (1967). Protein A from Staphylococcus aureus. III. Reaction with rabbit γ-globulin. Journal of Immunology 99, 1924.Google Scholar
Gladstone, G. P., Walton, E. & Kay, U. (1974). The effect of cultural conditions on the susceptibility of staphylococci to killing by the cationic proteins from rabbit polymorphonuclear leukocytes. British Journal of Experimental Pathology 55, 427447.Google Scholar
Hale, J. H. & Smith, W. (1945). The influence of coagulase on the phagocytosis of staphylococci. British Journal of Experimental Pathology 26, 209216.Google Scholar
Hawiger, J., Collins, R. D. & Horn, R. G. (1969). Precipitation of soluble fibrin monomer complexes by lysosomal protein fraction of polymorphonuclear leukocytes. Proceedings of the Society for Experimental Biology and Medicine 131, 349353.CrossRefGoogle ScholarPubMed
Hawiger, J., Hawioer, A. & Koenio, M. G. (1971). Staphylococcal clumping and fibrinogen and fibrin degradation products in inflammatory exudate. Proceedings of the Society for Experimental Biology and Medicine 136, 132136.Google Scholar
Hibbit, K. G. & Benians, M. (1973). The use of fluorescent conjugates to study the site of action of antimicrobial cationic proteins on staphylococci. Research in Veterinary Science 15, 6164.Google Scholar
Horn, R. G., Hawioer, J. & Collins, R. D. (1969). Electron microscopy of fibrin-like precipitate formed during the paracoagulation reaction between soluble fibrin monomer complexes and protamine sulphate. British Journal of Haematology 17, 463466.CrossRefGoogle ScholarPubMed
Kapral, F. A. & Li, I. W. (1960). Virulence and coagulases of Staphylococcus aureus. Proceedings of the Society for Experimental Biology and Medicine 104, 151155.CrossRefGoogle ScholarPubMed
Kolawole, D. O. (1983). Evaluation and use of the drug-inhibition method of measuring intracellular killing in differentiating between staphylococci grown in vivo and in vitro. Journal of Hygiene 91, 211222.CrossRefGoogle ScholarPubMed
Lipinski, B., Hawioer, J. & Jeljaszewicz, J. (1967). Staphylococcal clumping with soluble fibrin monomer complexes. Journal of Experimental Medicine 12, 979983.Google Scholar
Pennial, R., Hollbrook, J. P. & Zeya, H. I. (1972). The inhibition of cytochrome oxidase by lysosomal cationic proteins of rabbit polymorphonuclear leukocytes. Biochemistry and Biophysics Research Communications 47, 12701276.Google Scholar
Rogers, D. E. & Tompsett, R. (1952). The survival of staphylococci within human leukocytes. Journal of Experimental Medicine 95, 209230.Google Scholar
Yoshida, K., Ohtomo, T. & Minegishi, T. (1975). Extraction of a compact-colony forming activesubstancefrom Staphylococcus aureus strains. Japanese Journal of Microbiology 19, 7576.CrossRefGoogle ScholarPubMed
Yoshida, K., Ohtomo, T. & Minegishi, T. (1977). Mechanisms of compact-colony formation by strains of Staphylococcus aureus in serum soft agar. Journal of General Microbiology 98, 6775.Google Scholar
Yoshida, K., Ohtomo, T. & Usui, Y. (1978). Interaction of an alkali stable polysaccharide from cell surface of staphylococci with human fibrinogen. Experimentia 34, 885886.Google Scholar
Yoshida, K., Takahashi, M., Haga, K., Kono, E., Kushiro, H. & Ito, S. (1980). Comparison of three blood-clotting substances in Staphylococcus aureus strains. Journal of Clinical Microbiology 11, 293294.CrossRefGoogle ScholarPubMed