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. 1986 Jun;52(3):885–891. doi: 10.1128/iai.52.3.885-891.1986

Siderophore-mediated iron acquisition from transferrin by Pseudomonas aeruginosa.

S Sriyosachati, C D Cox
PMCID: PMC260943  PMID: 2940187

Abstract

Pseudomonas aeruginosa placed across a dialysis membrane from [55Fe]transferrin caused the mobilization of the iron from the transferrin side to the bacterial or dialysate side of the membrane. Although the bacteria were capable of obtaining iron from transferrin for growth, the siderophores of P. aeruginosa failed to convert iron bound to transferrin into dialyzable, low-molecular-weight chelates. The crucial factor produced by the bacteria which was not present when the siderophores were added alone was the acid produced from the glucose minimal medium. The siderophores mobilized considerable iron from transferrin when used in the dialysis assay at pH values between 5.0 and 6.0, values which were commonly found during incubation of bacteria in the assays. When the siderophores were tested individually, pyoverdin was more effective than pyochelin in mobilizing iron across dialysis membranes at pH values of 5.0 and 6.0, but neither had appreciable activity at pH 7.4. The amounts of iron mobilized from conalbumin were comparable to the amounts from transferrin, but there was negligible release from lactoferrin at the three pH values. When the two siderophores were combined, the level of iron mobilization was identical to that demonstrated by pyoverdin alone. When the dialysis membrane was removed and the bacteria were mixed with the siderophores and transferrin, pyoverdin was again more active than pyochelin in mediating iron transport. Although no pyochelin-mediated iron mobilization could be detected at pH 7.4, there was transport. Therefore, the bacteria appeared to be aiding the siderophores in iron mobilization from transferrin.

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Selected References

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  1. Aisen P. Citrate-mediated exchange of FE3+ among tranferrin molecules. Biochem Biophys Res Commun. 1968 Jul 26;32(2):220–226. doi: 10.1016/0006-291x(68)90372-0. [DOI] [PubMed] [Google Scholar]
  2. Aisen P., Listowsky I. Iron transport and storage proteins. Annu Rev Biochem. 1980;49:357–393. doi: 10.1146/annurev.bi.49.070180.002041. [DOI] [PubMed] [Google Scholar]
  3. Ankenbauer R., Sriyosachati S., Cox C. D. Effects of siderophores on the growth of Pseudomonas aeruginosa in human serum and transferrin. Infect Immun. 1985 Jul;49(1):132–140. doi: 10.1128/iai.49.1.132-140.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bullen J. J. The significance of iron in infection. Rev Infect Dis. 1981 Nov-Dec;3(6):1127–1138. doi: 10.1093/clinids/3.6.1127. [DOI] [PubMed] [Google Scholar]
  5. Carter P. Spectrophotometric determination of serum iron at the submicrogram level with a new reagent (ferrozine). Anal Biochem. 1971 Apr;40(2):450–458. doi: 10.1016/0003-2697(71)90405-2. [DOI] [PubMed] [Google Scholar]
  6. Costerton J. W., Lam J., Lam K., Chan R. The role of the microcolony mode of growth in the pathogenesis of Pseudomonas aeruginosa infections. Rev Infect Dis. 1983 Nov-Dec;5 (Suppl 5):S867–S873. doi: 10.1093/clinids/5.supplement_5.s867. [DOI] [PubMed] [Google Scholar]
  7. Cox C. D., Adams P. Siderophore activity of pyoverdin for Pseudomonas aeruginosa. Infect Immun. 1985 Apr;48(1):130–138. doi: 10.1128/iai.48.1.130-138.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cox C. D. Effect of pyochelin on the virulence of Pseudomonas aeruginosa. Infect Immun. 1982 Apr;36(1):17–23. doi: 10.1128/iai.36.1.17-23.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. Cox C. D. Iron transport and serum resistance in Pseudomonas aeruginosa. Antibiot Chemother (1971) 1985;36:1–12. doi: 10.1159/000410466. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. 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]
  13. Konopka K., Neilands J. B. Effect of serum albumin on siderophore-mediated utilization of transferrin iron. Biochemistry. 1984 May 8;23(10):2122–2127. doi: 10.1021/bi00305a003. [DOI] [PubMed] [Google Scholar]
  14. Lestas A. N. The effect of pH upon human transferrin: selective labelling of the two iron-binding sites. Br J Haematol. 1976 Mar;32(3):341–350. doi: 10.1111/j.1365-2141.1976.tb00937.x. [DOI] [PubMed] [Google Scholar]
  15. Liu P. V., Shokrani F. Biological activities of pyochelins: iron-chelating agents of Pseudomonas aeruginosa. Infect Immun. 1978 Dec;22(3):878–890. doi: 10.1128/iai.22.3.878-890.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Mickelsen P. A., Sparling P. F. Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from transferrin and iron compounds. Infect Immun. 1981 Aug;33(2):555–564. doi: 10.1128/iai.33.2.555-564.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Mietzner T. A., Luginbuhl G. H., Sandstrom E., Morse S. A. Identification of an iron-regulated 37,000-dalton protein in the cell envelope of Neisseria gonorrhoeae. Infect Immun. 1984 Aug;45(2):410–416. doi: 10.1128/iai.45.2.410-416.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Neilands J. B. Microbial iron compounds. Annu Rev Biochem. 1981;50:715–731. doi: 10.1146/annurev.bi.50.070181.003435. [DOI] [PubMed] [Google Scholar]
  19. O'Brien I. G., Gibson F. The structure of enterochelin and related 2,3-dihydroxy-N-benzoylserine conjugates from Escherichia coli. Biochim Biophys Acta. 1970 Aug 14;215(2):393–402. doi: 10.1016/0304-4165(70)90038-3. [DOI] [PubMed] [Google Scholar]
  20. Simonson C., Brener D., DeVoe I. W. Expression of a high-affinity mechanism for acquisition of transferrin iron by Neisseria meningitidis. Infect Immun. 1982 Apr;36(1):107–113. doi: 10.1128/iai.36.1.107-113.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Smith H. W. A search for transmissible pathogenic characters in invasive strains of Escherichia coli: the discovery of a plasmid-controlled toxin and a plasmid-controlled lethal character closely associated, or identical, with colicine V. J Gen Microbiol. 1974 Jul;83(0):95–111. doi: 10.1099/00221287-83-1-95. [DOI] [PubMed] [Google Scholar]
  22. Stuart S. J., Greenwood K. T., Luke R. K. Hydroxamate-mediated transport of iron controlled by ColV plasmids. J Bacteriol. 1980 Jul;143(1):35–42. doi: 10.1128/jb.143.1.35-42.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Warner P. J., Williams P. H., Bindereif A., Neilands J. B. ColV plasmid-specific aerobactin synthesis by invasive strains of Escherichia coli. Infect Immun. 1981 Aug;33(2):540–545. doi: 10.1128/iai.33.2.540-545.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Weinberg E. D. Iron and susceptibility to infectious disease. Science. 1974 May 31;184(4140):952–956. doi: 10.1126/science.184.4140.952. [DOI] [PubMed] [Google Scholar]
  25. Williams H. L., Conrad M. E. A one-tube method for measuring the serum iron concentration and unsaturated iron-binding capacity. J Lab Clin Med. 1966 Jan;67(1):171–176. [PubMed] [Google Scholar]
  26. Woods D. E., Bass J. A., Johanson W. G., Jr, Straus D. C. Role of adherence in the pathogenesis of Pseudomonas aeruginosa lung infection in cystic fibrosis patients. Infect Immun. 1980 Dec;30(3):694–699. doi: 10.1128/iai.30.3.694-699.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Yancey R. J., Finkelstein R. A. Siderophore production by pathogenic Neisseria spp. Infect Immun. 1981 May;32(2):600–608. doi: 10.1128/iai.32.2.600-608.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]

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