Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1985 Jun;162(3):1329–1331. doi: 10.1128/jb.162.3.1329-1331.1985

Genetic mapping and characterization of Pseudomonas aeruginosa mutants that hyperproduce exoproteins.

A Björklind, B Wretlind, I Möllegård, P A Schad, B H Iglewski, C D Cox
PMCID: PMC215928  PMID: 3922951

Abstract

We isolated two mutants of Pseudomonas aeruginosa PAO with defective iron uptake. In contrast to the wild-type strain, the mutants produced extracellular protease activity in media containing high concentrations of salts or iron and hyperproduced elastase, staphylolytic enzyme, and exotoxin A in ordinary media (Xch mutants). The mutations were located in the 55' region of the chromosome, between the markers met-9011 and pyrD.

Full text

PDF
1329

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Armstrong A. V., Stewart-Tull D. E., Roberts J. S. Characterisation of the Pseudomonas aeruginosa factor that inhibits mouse-liver mitochondrial respiration. J Med Microbiol. 1971 May;4(2):249–262. doi: 10.1099/00222615-4-2-249. [DOI] [PubMed] [Google Scholar]
  2. Berka R. M., Gray G. L., Vasil M. L. Studies of phospholipase C (heat-labile hemolysin) in Pseudomonas aeruginosa. Infect Immun. 1981 Dec;34(3):1071–1074. doi: 10.1128/iai.34.3.1071-1074.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bjorn M. J., Sokol P. A., Iglewski B. H. Influence of iron on yields of extracellular products in Pseudomonas aeruginosa cultures. J Bacteriol. 1979 Apr;138(1):193–200. doi: 10.1128/jb.138.1.193-200.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cox C. D., Graham R. Isolation of an iron-binding compound from Pseudomonas aeruginosa. J Bacteriol. 1979 Jan;137(1):357–364. doi: 10.1128/jb.137.1.357-364.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cox C. D. Iron uptake with ferripyochelin and ferric citrate by Pseudomonas aeruginosa. J Bacteriol. 1980 May;142(2):581–587. doi: 10.1128/jb.142.2.581-587.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cox C. D., Rinehart K. L., Jr, Moore M. L., Cook J. C., Jr Pyochelin: novel structure of an iron-chelating growth promoter for Pseudomonas aeruginosa. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4256–4260. doi: 10.1073/pnas.78.7.4256. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. DAVIS B. D., MINGIOLI E. S. Mutants of Escherichia coli requiring methionine or vitamin B12. J Bacteriol. 1950 Jul;60(1):17–28. doi: 10.1128/jb.60.1.17-28.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Haas D., Holloway B. W. Chromosome mobilization by the R plasmid R68.45: a tool in Pseudomonas genetics. Mol Gen Genet. 1978 Jan 17;158(3):229–237. doi: 10.1007/BF00267194. [DOI] [PubMed] [Google Scholar]
  9. Holloway B. W., Krishnapillai V., Morgan A. F. Chromosomal genetics of Pseudomonas. Microbiol Rev. 1979 Mar;43(1):73–102. doi: 10.1128/mr.43.1.73-102.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Ichida T., Osaka T., Kojima K. A simple method for the determination of serum iron. Clin Chim Acta. 1968 Oct;22(2):271–275. doi: 10.1016/0009-8981(68)90367-7. [DOI] [PubMed] [Google Scholar]
  11. Jensen S. E., Fecycz I. T., Campbell J. N. Nutritional factors controlling exocellular protease production by Pseudomonas aeruginosa. J Bacteriol. 1980 Nov;144(2):844–847. doi: 10.1128/jb.144.2.844-847.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kreger A. S., Griffin O. K. Physicochemical fractionation of extracellular cornea-damaging proteases of Pseudomonas aeruginosa. Infect Immun. 1974 May;9(5):828–834. doi: 10.1128/iai.9.5.828-834.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Laurell C. B. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem. 1966 Apr;15(1):45–52. doi: 10.1016/0003-2697(66)90246-6. [DOI] [PubMed] [Google Scholar]
  14. Liu P. V., Hsieh H. C. Inhibition of protease production of various bacteria by ammonium salts: its effect on toxin production and virulence. J Bacteriol. 1969 Aug;99(2):406–413. doi: 10.1128/jb.99.2.406-413.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Morihara K., Tsuzuki H. Production of protease and elastase by Pseudomonas aeruginosa strains isolated from patients. Infect Immun. 1977 Mar;15(3):679–685. doi: 10.1128/iai.15.3.679-685.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Philson S. B., Llinás M. Siderochromes from Pseudomonas fluorescens. I. Isolation and characterization. J Biol Chem. 1982 Jul 25;257(14):8081–8085. [PubMed] [Google Scholar]
  17. Sokol P. A., Cox C. D., Iglewski B. H. Pseudomonas aeruginosa mutants altered in their sensitivity to the effect of iron on toxin A or elastase yields. J Bacteriol. 1982 Aug;151(2):783–787. doi: 10.1128/jb.151.2.783-787.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Watson J. M., Holloway B. W. Suppressor mutations in Pseudomonas aeruginosa. J Bacteriol. 1976 Mar;125(3):780–786. doi: 10.1128/jb.125.3.780-786.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Woods D. E., Iglewski B. H. Toxins of Pseudomonas aeruginosa: new perspectives. Rev Infect Dis. 1983 Sep-Oct;5 (Suppl 4):S715–S722. doi: 10.1093/clinids/5.supplement_4.s715. [DOI] [PubMed] [Google Scholar]
  20. Wretlind B., Pavlovskis O. R. Genetic mapping and characterization of Pseudomonas aeruginosa mutants defective in the formation of extracellular proteins. J Bacteriol. 1984 Jun;158(3):801–808. doi: 10.1128/jb.158.3.801-808.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Wretlind B., Pavlovskis O. R. Pseudomonas aeruginosa elastase and its role in pseudomonas infections. Rev Infect Dis. 1983 Nov-Dec;5 (Suppl 5):S998–1004. doi: 10.1093/clinids/5.supplement_5.s998. [DOI] [PubMed] [Google Scholar]
  22. Wretlind B., Sjöberg L., Wadström T. Protease-deficient mutants of Pseudomonas aeruginosa: pleiotropic changes in activity of other extracellular enzymes. J Gen Microbiol. 1977 Dec;103(2):329–336. doi: 10.1099/00221287-103-2-329. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES