1887

Abstract

Summary: A heavy-metal-accumulating sp. has been used for the treatment of metal-laden industrial wastes. Metal uptake is mediated via a cell-bound phosphatase that liberates inorganic phosphate which precipitates with heavy metals as cell-bound metal phosphate. A phosphatase-deficient mutant accumulated little UO , while a phosphatase-overproducing mutant accumulated correspondingly more metal, with a uranium loading equivalent to the bacterial dry weight achieved after 6 h exposure of resting cells to uranyl ion in the presence of phosphatase substrate (glycerol 2-phosphate). The phosphatase, visualized by immunogold labelling in the parent and overproducing strains, but not seen in the deficient mutant, was held within the periplasmic space with, in some cells, a higher concentration at the polar regions. Enzyme was also associated with the outer membrane and found extracellularly. Accumulated uranyl phosphate was visible as cell-surface- and polar-localized deposits, identified by energy-dispersive X-ray analysis (EDAX), proton-induced X-ray emission analysis (PIXE) and X-ray diffraction analysis (XRD) as polycrystalline HUOPO.4HO. Nuclaation sites for initiation of biocrystallization were identified at the cytoplasmic and outer membranes, prompting consideration of an biocatalytic system for metal waste remediation. Phosphatidylcholine-based liposomes with entrapped phosphatase released phosphate comparably to whole cells, as shown by 31P NMR spectroscopy in the presence of ‘IMMR-silent’ Cd. Application of liposome-immobilized enzyme to the decontamination of uranyl solutions was, however, limited by rapid fouling of the biocatalyst by deposited uranyl phosphate. It is suggested that the architecture of the bacterial cell surface provides a means of access of uranyl ion to the inner and outer membranes and enzymically liberated phosphate in a way that minimizes fouling in whole cells.

Funding
This study was supported by the:
  • State and Hatch funds appropriated to the University of Georgia, College of Agriculture & Environmental Sciences Experiment Stations
Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-143-7-2509
1997-07-01
2021-08-06
Loading full text...

Full text loading...

/deliver/fulltext/micro/143/7/mic-143-7-2509.html?itemId=/content/journal/micro/10.1099/00221287-143-7-2509&mimeType=html&fmt=ahah

References

  1. Aisen P., Listowsky I. 1980; Iron transport and storage proteins. Annu Rev Biochem 49:357–393
    [Google Scholar]
  2. Ankenbauer R., Stiyosachati S., Cox C. D. 1985; Effects of siderophores on the growth of Pseudomonas aeruginosa in human serum and transferrin. Infect Immun 49:132–140
    [Google Scholar]
  3. Barclay R. 1985; The role of iron in infection. Med Lab Sci 42:166–177
    [Google Scholar]
  4. Bezkorovainy A. 1987 Iron proteins. . In Iron and Infection , pp. 27–67 . Edited by Bullen J. J., Griffiths E. New York: John Wiley;
    [Google Scholar]
  5. Bradford M. M. 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
    [Google Scholar]
  6. Bullen J. J., Armstrong J. A. 1979; The role of lactoferrin in the bacteriocidal function of polymorphonuclear leukocytes. Immunology 36:781–791
    [Google Scholar]
  7. Cornelis P., Hohnadel D., Meyer J. M. 1989; Evidence for different pyoverdin-mediated iron uptake systems among Pseudomonas aeruginosa strains. Infect Immun 57:3491–3497
    [Google Scholar]
  8. Cox C. D., Graham R. 1979; Isolation of an iron-binding compound from Pseudomonas aeruginosa . J Bacteriol 137:357–364
    [Google Scholar]
  9. Crichton R. R., Charloteaux-Wauters M. 1987; Iron transport and storage. Eur J Biochem 164:485–506
    [Google Scholar]
  10. Demange P., Wendenbaum S., Linget C., Mertz C., Cung M. T., Dell A., Abdallah M. A. 1990; Bacterial siderophores: structure and NMR assignment of pyoverdins Pa, siderophores of Pseudomonas aeruginosa ATCC 15692. Biol Metals 3:155–170
    [Google Scholar]
  11. Doggett R. G., Harrison G. M., Stillwell R. N., Wallis E. S. 1966; An atypical Pseudomonas aeruginosa associated with cystic fibrosis of the pancreas. J Pediatr 68:215–221
    [Google Scholar]
  12. Döring G., Pfestorf M., Botzenhart K., Abdallah M. A. 1988; Impact of proteases on iron uptake of Pseudomonas aeruginosa pyoverdin from transferrin and lactoferrin. Infect Immun 56:291–293
    [Google Scholar]
  13. Finkeistein R. A., Sciortino C. V., McIntosh M. A. 1983; Role of iron in microbe–host interaction. Rev Infect Dis 5:S759–S777
    [Google Scholar]
  14. Haas B., Kraut J., Marks J., Zanker S. C., Castignetti D. 1991a; Siderophore presence in sputa of cystic fibrosis patients. Infect Immun 59:3997–4000
    [Google Scholar]
  15. Haas B., Murphy E., Castignetti D. 1991b; Siderophore synthesis by mucoid Pseudomonas aeruginosa strains isolated from cystic fibrosis patients. Can J Microbiol 37:654–657
    [Google Scholar]
  16. Lankford C. E. 1973; Bacterial assimilation of iron. Crit Rev Microbiol 2:273–331
    [Google Scholar]
  17. Meyer J.-M., Neely A., Stintzi A., George C., Holder I. A. 1996; Pyoverdin is essential for virulence of Pseudomonas aeruginosa . Infect Immun 64:518–523
    [Google Scholar]
  18. Reynolds H. Y., Di Sant’Agnese P. A., Zierdt C. H. 1976; Mucoid Pseudomonas aeruginosa: a sign of cystic fibrosis in young adults with chronic pulmonary disease?. J Am Med Assoc 236:2190–2192
    [Google Scholar]
  19. Sriyosachati S., Cox C. D. 1986; Siderophore-mediated iron acquisition from transferrin by Pseudomonas aeruginosa . Infect Immun 52:885–891
    [Google Scholar]
  20. Stookey L. L. 1970; Ferrozine – a new spectrophotometric reagent for iron. Anal Chem 42:779–781
    [Google Scholar]
  21. Weinberg E. D. 1974; Iron and susceptibility to infectious disease. Science 184:952–956
    [Google Scholar]
  22. Weinberg E. D. 1978; Iron and infection. Microbial Rev 42:45–66
    [Google Scholar]
  23. Wendenbaum S., Demange P., Dell A., Meyer J. M., Abdallah M. A. 1983; The structure of pyoverdine Pa, the siderophore of Pseudomonas aeruginosa . Tetrahedron Lett 24:4877–4880
    [Google Scholar]
  24. Wolz C., Hohloch K., Octaktan A., Poole K., Evans R. W., Rochel N., Albrecht-Gary A. M., Abdallah M. A., Döring G. 1994; Iron release from transferrin by pyoverdin and elastase from Pseudomonas aeruginosa . Infect Immun 62:4021–4027
    [Google Scholar]
  25. Xiao R., Kisaalita W. S. 1995; Purification of pyoverdines of Pseudomonas fluorescens 2-79 by copper chelate chromatography. Appl Environ Microbiol 61:3769–3774
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-143-7-2509
Loading
/content/journal/micro/10.1099/00221287-143-7-2509
Loading

Data & Media loading...

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