1887

Abstract

Mutants of strain -1 which are defective in the formation of extracellular protease activity have been characterized. The mutants produced between approximately 1 and 25 % of the protease activity of the wild type and no strains completely lacking extracellular protease were found, even after repeated mutagen treatment. Most mutants also had changed activities of extracellular staphylolytic enzyme, lipase and lecithinase. Four of 13 mutants were unable to release alkaline phosphatase and staphylolytic enzyme into the medium in contrast to the wild type. Serotype, phage type and biochemical reactions were essentially unchanged. The results indicate that some of the mutations affected the cell envelope structure or function leading to decreased ability to release extracellular proteins, and that other mutations possibly affected a common regulatory mechanism for extracellular enzymes.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-103-2-329
1977-12-01
2021-10-17
Loading full text...

Full text loading...

/deliver/fulltext/micro/103/2/mic-103-2-329.html?itemId=/content/journal/micro/10.1099/00221287-103-2-329&mimeType=html&fmt=ahah

References

  1. Altenbern R. A. 1975; Membrane mutations and production of enterotoxin B and alpha hemolysin in Staphylococcus aureus. Canadian Journal of Microbiology 21:275–280
    [Google Scholar]
  2. Arvidson S., Holme T., Wadström T. 1971; Influence of cultivation conditions on the production of extracellular proteins by Staphylococcus aureus. Acta pathologica et microbiologica scandinavica B79:399–405
    [Google Scholar]
  3. Burke M. E., Pattee P. A. 1967; Purification and characterization of a staphylolytic enzyme from Pseudomonas aeruginosa. Journal of Bacteriology 93:860–866
    [Google Scholar]
  4. Cheng K.-J., Ingram J. M., Costerton J. W. 1971; Interactions of alkaline phosphatase and the cell wall of Pseudomonas aeruginosa. Journal of Bacteriology 107:325–336
    [Google Scholar]
  5. Davis B. D., Mingioli E. S. 1950; Mutants of Escherichia coli requiring methionine or vitamin B12. Journal of Bacteriology 60:17–28
    [Google Scholar]
  6. Ericsson H. M., Sherris J. C. 1971; Antibiotic sensitivity testing. Report of an international collaborative study. Acta pathologica et microbiologica scandinavica B, Supplement 217:
    [Google Scholar]
  7. Forsgren A., Nordström K., Philipson L., Sjöquist J. 1971; Protein A mutants of Staphylococcus aureus. Journal of Bacteriology 107:245–250
    [Google Scholar]
  8. Habs I. 1957; Untersuchungen über die O-Antigene von Pseudomonas aeruginosa. Zeitschrift für Hygiene und Infektionskrankheiten 144:218–228
    [Google Scholar]
  9. Holloway B. W. 1975; Genetic organization of Pseudomonas. In Genetics and Biochemistry of Pseudomonas pp. 133–161 Clarke P. H., Richmond M. H. Edited by London: John Wiley;
    [Google Scholar]
  10. Hugh R., Gelardi G. L. 1974 Pseudomonas. In Manual of Clinical Microbiology, 2nd edn.. pp. 250–269 Lennette E. H., Spaulding E. H., Truant J. P. Edited by Washington, D.C.: American Society for Microbiology;
    [Google Scholar]
  11. Kawaharajo K., Homma J. Y., Aoyama Y., Morihara K. 1975; In vivo studies on protease and elastase from Pseudomonas aeruginosa. Japanese Journal of Experimental Medicine 45:89–100
    [Google Scholar]
  12. Kreger A. S., Griffin O. K. 1974; Physicochemical fractionation of extracellular corneadamaging proteases of Pseudomonas aeruginosa. Infection and Immunity 9:828–834
    [Google Scholar]
  13. Kunitz M. 1946/1947; Crystalline soybean trypsin inhibitor. II. General properties. Journal of General Physiology 30:291–310
    [Google Scholar]
  14. Liu P. V. 1964; Factors that influence toxigenicity of Pseudomonas aeruginosa. Journal of Bacteriology 88:1421–1427
    [Google Scholar]
  15. Liu P. V. 1974; Extracellular toxins of Pseudomonas aeruginosa. Journal of Infectious Diseases 130: Supplement S94–S99
    [Google Scholar]
  16. Maliwan N., Hess A. R., Grieble H. G., Bird T. J. 1974; Curing of carbenicillinase mediated resistance in Pseudomonas aeruginosa. In Progress in Chemotherapy 1 pp. 186–192 Daikos G. K. Edited by Athens: Hellenic Society of Chemotherapy;
    [Google Scholar]
  17. Meynell C. G., Meynell E. 1970; Genetic technique. In Theory and Practice in Experimental Bacteriology, 2nd edn.. pp. 256–294 London: Cambridge University Press;
    [Google Scholar]
  18. Morihara K. 1964; Production of elastase and proteinase by Pseudomonas aeruginosa. Journal of Bacteriology 88:745–757
    [Google Scholar]
  19. Mull J. D., Callahan W. S. 1965; The role of the elastase of Pseudomonas aeruginosa in ex-perimental infection. Experimental and Molecular Pathology 4:567–575
    [Google Scholar]
  20. Omenn G. S., Friedman J. 1970; Isolation of mutants of Staphylococcus aureus lacking extracellular nuclease activity. Journal of Bacteriology 101:921–924
    [Google Scholar]
  21. Praglin J., Curtiss A. C., Longhenry D. K., Mckie J.E. Jr 1975; Autobac 1-A 3-hours, automated antimicrobial susceptibility system. I. System description. In Automation in Microbiology and Immunology pp. 197–208 Hedén C.-G., Illéni T. Edited by New York: John Wiley;
    [Google Scholar]
  22. Rudin L., V.Hofsten B. 1974; Mutations in Arthrobacter affecting the formation of extracellular protease. Acta pathologica et microbiologica scandinavica B82:657–666
    [Google Scholar]
  23. Sjöberg L., Lindberg A. A. 1968; Phage typing of Pseudomonas aeruginosa. Acta pathologica et microbiologica scandinavica 74:61–68
    [Google Scholar]
  24. So M., Crandall J. F., Crosa J. H., Falkow S. 1975; Extrachromosomal determinants which contribute to bacterial pathogenicity. In Microbiology - 1974 pp. 16–26 Schlessinger D. Edited by Washington, D.C.: American Society for Microbiology;
    [Google Scholar]
  25. Staeudinger M., V.Diemling O., Grossarth C., Wienker T. 1973; Esterase. VIII. Histo- chemische, elektrophoretische und quantitative Untersuchungen zum Einfluss von Phenobarbital auf die Leberesterase der Maus. Histochemie 34:107–116
    [Google Scholar]
  26. Torriani A. 1968; Alkaline phosphatase of Escherichia coli. Methods in Enzymology 12B:212–218
    [Google Scholar]
  27. Vera H. D., Dumoff M. 1974; Culture media. In Manual of Clinical Microbiology, 2nd edn.. pp. 881–929 Lennette E. H., Spaulding E. H., Truant J. P. Edited by Washington, D.C. : American Society for Microbiology;
    [Google Scholar]
  28. Wadström T. 1973; Bacteriolytic enzymes from staphylococci. In Staphylococci and Staphylococcal Infections pp. 397–405 Jeljaszewicz J. Edited by Basel: Karger;
    [Google Scholar]
  29. Winkler U., Timmis K. 1973; Pleiotropic mutations in Serratia marcescens which increase the synthesis of certain exocellular proteins and the rate of spontaneous prophage induction. Molecular and General Genetics 124:197–206
    [Google Scholar]
  30. Wretlind B., Wadström T. 1977; Purification and properties of a protease with elastase activity from Pseudomonas aeruginosa. Journal of General Microbiology 103:319–327
    [Google Scholar]
  31. Wretlind B., HedÉn L., Sjöberg L., Wadström T. 1973; Production of enzymes and toxins by hospital strains of Pseudomonas aeruginosa in relation to serotype and phage-typing pattern. Journal of Medical Microbiology 6:91–100
    [Google Scholar]
  32. Yoshikawa M., Matsuda F., Naka M., Muro-Fushi E., Tsunematsu Y. 1974; Pleiotropic alteration of activities of several toxins and enzymes in mutants of Staphylococcus aureus. Journal of Bacteriology 119:117–122
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-103-2-329
Loading
/content/journal/micro/10.1099/00221287-103-2-329
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error