This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bramanti, T E
Right arrow Articles by Holt, S C
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bramanti, T E
Right arrow Articles by Holt, S C

 Previous Article  |  Next Article 

J Bacteriol. 1991 November; 173(22): 7330-7339

research-article

Roles of porphyrins and host iron transport proteins in regulation of growth of Porphyromonas gingivalis W50.

T E Bramanti and S C Holt

University of Texas Health Science Center, San Antonio 78284-7894.

ABSTRACT

Porphyromonas gingivalis (Bacteroides gingivalis) requires iron in the form of hemin for growth and virulence in vitro, but the contributions of the porphyrin ring structure, porphyrin-associated iron, host hemin-sequestering molecules, and host iron-withholding proteins to its survival are unknown. Therefore, the effects of various porphyrins, host iron transport proteins, and inorganic iron sources on the growth of P. gingivalis W50 were examined to delineate the various types of iron molecules used for cellular metabolism. Cell envelope-associated hemin and iron stores contributed to the growth of P. gingivalis in hemin-free culture, and depletion of these endogenous reserves required eight serial transfers into hemin-free medium for total suppression of growth. Comparable growth of P. gingivalis was observed with 7.7 microM equivalents of hemin as hemoglobin (HGB), methemoglobin, myoglobin, hemin-saturated serum albumin, lactoperoxidase, cytochrome c, and catalase. Unrestricted growth was recorded in the presence of haptoglobin-HGB and hemopexin-hemin complexes, indicating that these host defense proteins do not sequester HGB and hemin from P. gingivalis. The iron chelator 2,2'-bipyridyl functionally chelated hemin-associated iron, resulting in dose-dependent inhibition of growth in hemin-restricted cultures at 1 to 25 microM 2,2'-bipyridyl concentrations. In the absence of an exogenous iron source, protoporphyrin IX did not support P. gingivalis growth. These findings suggest that the iron atom in the hemin molecule is the critical constituent for growth and that the tetrapyrrole porphyrin ring structure may represent an important vehicle for delivery of iron into the P. gingivalis cell. P. gingivalis does not have a strict requirement for porphyrins, since growth occurred with nonhemin iron sources, including high concentrations (200 muM) of ferric, ferrous, and nitrogenous inorganic iron, and P. gingivalis exhibited unrestricted growth in the presence of host transferrin, lactoferrin, and serum albumin. The diversity of iron substrates utilized by P. gingivalis and the observation that growth was not affected by the bacteriostatic effects of host iron-withholding proteins, which it may encounter in the periodontal pocket, may explain why P. gingivalis is such a formidable pathogen in the periodontal disease process.

J Bacteriol. 1991 November; 173(22): 7330-7339




This article has been cited by other articles:

  • Dashper, S. G., Ang, C.-S., Veith, P. D., Mitchell, H. L., Lo, A. W. H., Seers, C. A., Walsh, K. A., Slakeski, N., Chen, D., Lissel, J. P., Butler, C. A., O'Brien-Simpson, N. M., Barr, I. G., Reynolds, E. C. (2009). Response of Porphyromonas gingivalis to Heme Limitation in Continuous Culture. J. Bacteriol. 191: 1044-1055 [Abstract] [Full Text]  
  • Kuramitsu, H. K., He, X., Lux, R., Anderson, M. H., Shi, W. (2007). Interspecies Interactions within Oral Microbial Communities. Microbiol. Mol. Biol. Rev. 71: 653-670 [Abstract] [Full Text]  
  • Shi, X., Hanley, S. A., Faray-Kele, M.-C., Fawell, S. C., Aduse-Opoku, J., Whiley, R. A., Curtis, M. A., Hall, L. M. C. (2007). The rag Locus of Porphyromonas gingivalis Contributes to Virulence in a Murine Model of Soft Tissue Destruction. Infect. Immun. 75: 2071-2074 [Abstract] [Full Text]  
  • Lewis, J. P., Plata, K., Yu, F., Rosato, A., Anaya, C. (2006). Transcriptional organization, regulation and role of the Porphyromonas gingivalis W83 hmu haemin-uptake locus.. Microbiology 152: 3367-3382 [Abstract] [Full Text]  
  • Liu, X., Olczak, T., Guo, H.-C., Dixon, D. W., Genco, C. A. (2006). Identification of Amino Acid Residues Involved in Heme Binding and Hemoprotein Utilization in the Porphyromonas gingivalis Heme Receptor HmuR. Infect. Immun. 74: 1222-1232 [Abstract] [Full Text]  
  • Dashper, S. G., Butler, C. A., Lissel, J. P., Paolini, R. A., Hoffmann, B., Veith, P. D., O'Brien-Simpson, N. M., Snelgrove, S. L., Tsiros, J. T., Reynolds, E. C. (2005). A Novel Porphyromonas gingivalis FeoB Plays a Role in Manganese Accumulation. J. Biol. Chem. 280: 28095-28102 [Abstract] [Full Text]  
  • DeCarlo, A. A., Huang, Y., Collyer, C. A., Langley, D. B., Katz, J. (2003). Feasibility of an HA2 Domain-Based Periodontitis Vaccine. Infect. Immun. 71: 562-566 [Abstract] [Full Text]  
  • Sroka, A., Sztukowska, M., Potempa, J., Travis, J., Genco, C. A. (2001). Degradation of Host Heme Proteins by Lysine- and Arginine-Specific Cysteine Proteinases (Gingipains) of Porphyromonas gingivalis. J. Bacteriol. 183: 5609-5616 [Abstract] [Full Text]  
  • Grenier, D., Goulet, V., Mayrand, D. (2001). The Capacity of Porphyromonas gingivalis to Multiply Under Iron-limiting Conditions Correlates with its Pathogenicity in an Animal Model. JDR 80: 1678-1682 [Abstract]  
  • Smalley, J. W., Charalabous, P., Birss, A. J., Hart, C. A. (2001). Detection of Heme-Binding Proteins in Epidemic Strains of Burkholderia cepacia. CVI 8: 509-514 [Abstract] [Full Text]  
  • Kuboniwa, M., Amano, A., Shizukuishi, S., Nakagawa, I., Hamada, S. (2001). Specific Antibodies to Porphyromonas gingivalis Lys-Gingipain by DNA Vaccination Inhibit Bacterial Binding to Hemoglobin and Protect Mice from Infection. Infect. Immun. 69: 2972-2979 [Abstract] [Full Text]  
  • Dashper, S. G., Hendtlass, A., Slakeski, N., Jackson, C., Cross, K. J., Brownfield, L., Hamilton, R., Barr, I., Reynolds, E. C. (2000). Characterization of a Novel Outer Membrane Hemin-Binding Protein of Porphyromonas gingivalis. J. Bacteriol. 182: 6456-6462 [Abstract] [Full Text]  
  • Lewis, J. P., Dawson, J. A., Hannis, J. C., Muddiman, D., Macrina, F. L. (1999). Hemoglobinase Activity of the Lysine Gingipain Protease (Kgp) of Porphyromonas gingivalis W83. J. Bacteriol. 181: 4905-4913 [Abstract] [Full Text]  
  • DeCarlo, A. A., Paramaesvaran, M., Yun, P. L. W., Collyer, C., Hunter, N. (1999). Porphyrin-Mediated Binding to Hemoglobin by the HA2 Domain of Cysteine Proteinases (Gingipains) and Hemagglutinins from the Periodontal Pathogen Porphyromonas gingivalis. J. Bacteriol. 181: 3784-3791 [Abstract] [Full Text]  
  • Kesavalu, L., Holt, S. C., Ebersole, J. L. (1999). Environmental Modulation of Oral Treponeme Virulence in a Murine Model. Infect. Immun. 67: 2783-2789 [Abstract] [Full Text]  
  • Duchesne, P., Grenier, D., Mayrand, D. (1999). Binding and Utilization of Human Transferrin by Prevotella nigrescens. Infect. Immun. 67: 576-580 [Abstract] [Full Text]  
  • Lamont, R. J., Jenkinson, H. F. (1998). Life Below the Gum Line: Pathogenic Mechanisms of Porphyromonas gingivalis. Microbiol. Mol. Biol. Rev. 62: 1244-1263 [Abstract] [Full Text]  
  • Genco, C.A. (1995). Regulation of Hemin and Iron Transport in Porphyromonas Gingivalis. ADR 9: 41-47 [Abstract]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»