1887

Abstract

Summary

Cysteine-dependent (cys) and spp., defective in sulphate assimilation, were isolated from urine and stool samples of infected patients. These isolates reverted to prototrophy under conditions of cysteine deprivation but the revertant strains and a prototrophic wild-type strain became auxotrophic for cysteine in a cysteine-enriched medium. This suggested that excess cysteine acts as a repressor of the operon known to control aspects of cysteine biosynthesis. A group of mostly elderly patients infected with cys strains suffered a disproportionate amount of renal impairment as compared with a control group. In renal impairment, sulphur compounds, including cysteine, are retained. This raises the possibility that these raised levels of cysteine and related compounds may enhance the selection of cys strains

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1993-11-01
2024-11-08
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References

  1. Borderon E, Horodniceanu T. Metabolically deficient dwarfcolony mutants of Escherichia coli: deficiency and resistance to antibiotics of strains isolated from urine culture. J Clin Microbiol 1978; 8:629–634
    [Google Scholar]
  2. Mclver CJ, Tapsall JW. Characteristics of cysteine-requiring strains of Klebsiella isolated from urinary tract infections. J Med Microbiol 1988; 26:211–215
    [Google Scholar]
  3. Tapsall JW, Mclver CJ. Septicaemia caused by cysteine- requiring isolates of Escherichia coli. J Med Microbiol 1986; 22:379–382
    [Google Scholar]
  4. Mclver CJ, Tapsall JW. Cysteine requirements of naturally occurring cysteine auxotrophs of Escherichia coli. Pathology 1987; 19:361–363
    [Google Scholar]
  5. Mclver CJ, Tapsall JW. Assessment of conventional and commercial methods for identification of clinical isolates of cysteine-requiring strains of Escherichia coli and Klebsiella species. J Clin Microbiol 1990; 28:1947–1951
    [Google Scholar]
  6. Mclver CJ, Tapsall JW. In vitro susceptibilities of clinical isolates of cysteine-requiring Escherichia coli to 12 antimicrobial agents. Antimicrob Agents Chemother 1991; 35:995–997
    [Google Scholar]
  7. Gillespie WA. Biochemical mutants of coliform bacilli in infections of the urinary tract. J Pathol Bacteriol 1952; 64:551–557
    [Google Scholar]
  8. Wilcken DEL, Gupta VJ. Sulphur containing amino acids in chronic renal failure with particular reference to homocysteine and cysteine-homocysteine mixed disulphide. Eur J Clin Invest 1979; 9:301–307
    [Google Scholar]
  9. Wilcken DEL, Gupta VJ, Betts AK. Homocysteine in the plasma of renal transplant recipients: effects of co-factors for methionine metabolism. Clin Sci 1981; 61:743–749
    [Google Scholar]
  10. Wilcken DEL, Gupta VJ, Reddy SG. Accumulation of sulphur- containing amino acids including cysteine-homocysteine in patients on maintenance haemodialysis. Clin Sci 1980; 58:427–430
    [Google Scholar]
  11. Davis BD. Isolation of biochemically deficient mutants of bacteria by penicillin. J Am Chem Soc 1948; 70:4267
    [Google Scholar]
  12. Davis BD, Mingioli ES. Mutants of Escherichia coli requiring methionine or vitamin B12. JBacteriol 1950; 60:17–28
    [Google Scholar]
  13. Jones-Mortimer MC. Positive control of sulphate reduction in Escherichia coli. Isolation, characterization and mapping of cysteineless mutants of E. coli K12. Biochem J 1968; 110:589–595
    [Google Scholar]
  14. Pasternak CA. Sulphate activation and its control in Escherichia coli and Bacillus subtilis. Biochem J 1962; 85:44–49
    [Google Scholar]
  15. Mizobuchi K., Demerec M, Gillespie DH. Cysteine mutants of Salmonella typhimurium. Genetics 1962; 47:1617–1627
    [Google Scholar]
  16. Kredich NM. Biosynthesis of cysteine. In: Neidhardt FC. (ed) Escherichia coli and Salmonella typhimurium: cellular and molecular biology vol 1 Washington, DC: American Society for Microbiology.; 1987419–428
    [Google Scholar]
  17. Dreyfuss J, Monty KJ. The biochemical characterization of cysteine-requiring mutants of Salmonella typhimurium. J Biol Chem 1963; 238:1019–1024
    [Google Scholar]
  18. Postgate JR. The examination of sulphur auxotrophs: a warning. J Gen Microbiol 1963; 30:481–484
    [Google Scholar]
  19. Parra F, Britton CP, Castle C, Jones-Mortimer MC, Komberg HL. Two separate genes involved in sulphate transport in Escherichia coli K12. J Gen Microbiol 1983; 129:357–358
    [Google Scholar]
  20. Bachmann BJ. Linkage map of Escherichia coli K12, edition 8. Microbiol Rev 1990; 54:130–197
    [Google Scholar]
  21. Jacob F, Monod J. Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol 1961; 3:318–356
    [Google Scholar]
  22. Perry TL, Hansen S. Technical pitfalls leading to errors in the quantitation of plasma amino acids. Clin Chim Acta 1969; 25:53–58
    [Google Scholar]
  23. Cooper JDH, Turnell DC, Green B, Wright DJ, Coombes EJ. Why the assay of serum cystine by protein precipitation should be abandoned. Ann Clin Biochem 1988; 25:577–582
    [Google Scholar]
  24. Schneider JA, Dalton RN. Why the assay of serum cystine by protein precipitation and chromatography should be abandoned. Ann Clin Chem 1989; 26:305–306
    [Google Scholar]
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