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. 1990 Dec;58(12):4016–4019. doi: 10.1128/iai.58.12.4016-4019.1990

Hemin levels in culture medium of Porphyromonas (Bacteroides) gingivalis regulate both hemin binding and trypsinlike protease production.

R J Carman 1, M D Ramakrishnan 1, F H Harper 1
PMCID: PMC313770  PMID: 2254026

Abstract

Washed cells and Sarkosyl-insoluble outer membrane preparations of the black-pigmented bacteroides Porphyromonas gingivalis W50 bound hemin. The amount of hemin removed from a buffered solution by both cells and outer membranes was significantly larger if bacteria had been grown in broths supplemented with 5 mg of hemin per liter rather than none. Conversely, cells grown without supplemental hemin bound relatively little. However, all preparations bound some hemin. In addition, hemin regulated the production of significantly higher levels of trypsinlike protease by P. gingivalis W50. The nonpigmented variant, W50 BE1, showed no such responses to the levels of hemin in the growth medium.

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Selected References

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  1. Carlone G. M., Thomas M. L., Rumschlag H. S., Sottnek F. O. Rapid microprocedure for isolating detergent-insoluble outer membrane proteins from Haemophilus species. J Clin Microbiol. 1986 Sep;24(3):330–332. doi: 10.1128/jcm.24.3.330-332.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Carlsson J., Höfling J. F., Sundqvist G. K. Degradation of albumin, haemopexin, haptoglobin and transferrin, by black-pigmented Bacteroides species. J Med Microbiol. 1984 Aug;18(1):39–46. doi: 10.1099/00222615-18-1-39. [DOI] [PubMed] [Google Scholar]
  3. Daskaleros P. A., Payne S. M. Congo red binding phenotype is associated with hemin binding and increased infectivity of Shigella flexneri in the HeLa cell model. Infect Immun. 1987 Jun;55(6):1393–1398. doi: 10.1128/iai.55.6.1393-1398.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Eaton J. W., Brandt P., Mahoney J. R., Lee J. T., Jr Haptoglobin: a natural bacteriostat. Science. 1982 Feb 5;215(4533):691–693. doi: 10.1126/science.7036344. [DOI] [PubMed] [Google Scholar]
  5. Haapasalo M., Shah H., Gharbia S., Seddon S., Lounatmaa K. Surface properties and ultrastructure of Porphyromonas gingivalis W50 and pleiotropic mutants. Scand J Dent Res. 1989 Aug;97(4):355–360. doi: 10.1111/j.1600-0722.1989.tb01623.x. [DOI] [PubMed] [Google Scholar]
  6. Ishiguro E. E., Ainsworth T., Trust T. J., Kay W. W. Congo red agar, a differential medium for Aeromonas salmonicida, detects the presence of the cell surface protein array involved in virulence. J Bacteriol. 1985 Dec;164(3):1233–1237. doi: 10.1128/jb.164.3.1233-1237.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Maiden M. F., Carman R. J., Curtis M. A., Gillett I. R., Griffiths G. S., Sterne J. A., Wilton J. M., Johnson N. W. Detection of high-risk groups and individuals for periodontal diseases: laboratory markers based on the microbiological analysis of subgingival plaque. J Clin Periodontol. 1990 Jan;17(1):1–13. doi: 10.1111/j.1600-051x.1990.tb01040.x. [DOI] [PubMed] [Google Scholar]
  8. Mansheim B. J., Kasper D. L. Purification and immunochemical characterization of the outer membrane complex of Bacteroides melaninogenicus subspecies asaccharolyticus. J Infect Dis. 1977 May;135(5):787–799. doi: 10.1093/infdis/135.5.787. [DOI] [PubMed] [Google Scholar]
  9. Marsh P. D., McKee A. S., McDermid A. S., Dowsett A. B. Ultrastructure and enzyme activities of a virulent and an avirulent variant of Bacteroides gingivalis W50. FEMS Microbiol Lett. 1989 May;50(1-2):181–185. doi: 10.1016/0378-1097(89)90482-5. [DOI] [PubMed] [Google Scholar]
  10. Mayrand D., Holt S. C. Biology of asaccharolytic black-pigmented Bacteroides species. Microbiol Rev. 1988 Mar;52(1):134–152. doi: 10.1128/mr.52.1.134-152.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Mayrand D., McBride B. C. Exological relationships of bacteria involved in a simple, mixed anaerobic infection. Infect Immun. 1980 Jan;27(1):44–50. doi: 10.1128/iai.27.1.44-50.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. McKee A. S., McDermid A. S., Wait R., Baskerville A., Marsh P. D. Isolation of colonial variants of Bacteroides gingivalis W50 with a reduced virulence. J Med Microbiol. 1988 Sep;27(1):59–64. doi: 10.1099/00222615-27-1-59. [DOI] [PubMed] [Google Scholar]
  13. Mukherjee S. The role of crevicular fluid iron in periodontal disease. J Periodontol. 1985 Nov;56(11 Suppl):22–27. doi: 10.1902/jop.1985.56.11s.22. [DOI] [PubMed] [Google Scholar]
  14. Sankaran K., Ramachandran V., Subrahmanyam Y. V., Rajarathnam S., Elango S., Roy R. K. Congo red-mediated regulation of levels of Shigella flexneri 2a membrane proteins. Infect Immun. 1989 Aug;57(8):2364–2371. doi: 10.1128/iai.57.8.2364-2371.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Shah H. N., Bonnett R., Mateen B., Williams R. A. The porphyrin pigmentation of subspecies of Bacteroides melaninogenicus. Biochem J. 1979 Apr 15;180(1):45–50. doi: 10.1042/bj1800045. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Shah H. N., Seddon S. V., Gharbia S. E. Studies on the virulence properties and metabolism of pleiotropic mutants of Porphyromonas gingivalis (Bacteroides gingivalis) W50. Oral Microbiol Immunol. 1989 Mar;4(1):19–23. doi: 10.1111/j.1399-302x.1989.tb00401.x. [DOI] [PubMed] [Google Scholar]
  17. Sikkema D. J., Brubaker R. R. Resistance to pesticin, storage of iron, and invasion of HeLa cells by Yersiniae. Infect Immun. 1987 Mar;55(3):572–578. doi: 10.1128/iai.55.3.572-578.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Simpson I. A., Sonne O. A simple, rapid, and sensitive method for measuring protein concentration in subcellular membrane fractions prepared by sucrose density ultracentrifugation. Anal Biochem. 1982 Jan 15;119(2):424–427. doi: 10.1016/0003-2697(82)90608-x. [DOI] [PubMed] [Google Scholar]
  19. Smalley J. W., Birss A. J., Kay H. M., McKee A. S., Marsh P. D. The distribution of trypsin-like enzyme activity in cultures of a virulent and an avirulent strain of Bacteroides gingivalis W50. Oral Microbiol Immunol. 1989 Sep;4(3):178–181. doi: 10.1111/j.1399-302x.1989.tb00249.x. [DOI] [PubMed] [Google Scholar]
  20. Sperry J. F., Appleman M. D., Wilkins T. D. Requirement of heme for growth of Bacteroides fragilis. Appl Environ Microbiol. 1977 Oct;34(4):386–390. doi: 10.1128/aem.34.4.386-390.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Stoebner J. A., Payne S. M. Iron-regulated hemolysin production and utilization of heme and hemoglobin by Vibrio cholerae. Infect Immun. 1988 Nov;56(11):2891–2895. doi: 10.1128/iai.56.11.2891-2895.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Stugard C. E., Daskaleros P. A., Payne S. M. A 101-kilodalton heme-binding protein associated with congo red binding and virulence of Shigella flexneri and enteroinvasive Escherichia coli strains. Infect Immun. 1989 Nov;57(11):3534–3539. doi: 10.1128/iai.57.11.3534-3539.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Stull T. L. Protein sources of heme for Haemophilus influenzae. Infect Immun. 1987 Jan;55(1):148–153. doi: 10.1128/iai.55.1.148-153.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]

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