This Article
Right arrow Full Text
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 Sroka, A.
Right arrow Articles by Genco, C. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sroka, A.
Right arrow Articles by Genco, C. A.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2001, p. 5609-5616, Vol. 183, No. 19
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.19.5609-5616.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Degradation of Host Heme Proteins by Lysine- and Arginine-Specific Cysteine Proteinases (Gingipains) of Porphyromonas gingivalis

Aneta Sroka,1,2 Maryta Sztukowska,2,3 Jan Potempa,2,3 James Travis,3 and Caroline Attardo Genco1,*

Section of Infectious Diseases, Department of Medicine, Boston University School of Medicine, Boston, Massachusetts 021181; Department of Microbiology, Institute of Molecular Biology, Jagiellonian University, 31-120 Crakow, Poland2; and Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 306023

Received 2 March 2001/Accepted 5 July 2001

Porphyromonas gingivalis can use hemoglobin bound to haptoglobin and heme complexed to hemopexin as heme sources; however, the mechanism by which hemin is released from these proteins has not been defined. In the present study, using a variety of analytical methods, we demonstrate that lysine-specific cysteine proteinase of P. gingivalis (gingipain K, Kgp) can efficiently cleave hemoglobin, hemopexin, haptoglobin, and transferrin. Degradation of hemopexin and transferrin in human serum by Kgp was also detected; however, we did not observe extensive degradation of hemoglobin in serum by Kgp. Likewise the beta -chain of haptoglobin was partially protected from degradation by Kgp in a haptoglobin-hemoglobin complex. Arginine-specific gingipains (gingipains R) were also found to degrade hemopexin and transferrin in serum; however, this was observed only at relatively high concentrations of these enzymes. Growth of P. gingivalis strain A7436 in a minimal media with normal human serum as a source of heme correlated not only with the ability of the organism to degrade hemoglobin, haptoglobin, hemopexin, and transferrin but also with an increase in gingipain K and gingipain R activity. The ability of gingipain K to cleave hemoglobin, haptoglobin, and hemopexin may provide P. gingivalis with a useable source of heme for growth and may contribute to the proliferation of P. gingivalis within periodontal pockets in which erythrocytes are abundant.

* Corresponding author. Mailing address: Department of Medicine, Section of Infectious Diseases, Boston University School of Medicine, 650 Albany St., Boston, MA 02118. Phone: (617) 414-5305. Fax: (617) 414-5280. E-mail: caroline.genco{at}bmc.org.

Journal of Bacteriology, October 2001, p. 5609-5616, Vol. 183, No. 19
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.19.5609-5616.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Wu, J., Lin, X., Xie, H. (2009). Regulation of Hemin Binding Proteins by a Novel Transcriptional Activator in Porphyromonas gingivalis. J. Bacteriol. 191: 115-122 [Abstract] [Full Text]  
  • Louvel, H., Bommezzadri, S., Zidane, N., Boursaux-Eude, C., Creno, S., Magnier, A., Rouy, Z., Medigue, C., Girons, I. S., Bouchier, C., Picardeau, M. (2006). Comparative and Functional Genomic Analyses of Iron Transport and Regulation in Leptospira spp.. J. Bacteriol. 188: 7893-7904 [Abstract] [Full Text]  
  • James, C. E., Hasegawa, Y., Park, Y., Yeung, V., Tribble, G. D., Kuboniwa, M., Demuth, D. R., Lamont, R. J. (2006). LuxS Involvement in the Regulation of Genes Coding for Hemin and Iron Acquisition Systems in Porphyromonas gingivalis. Infect. Immun. 74: 3834-3844 [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]  
  • Vanterpool, E., Roy, F., Fletcher, H. M. (2005). Inactivation of vimF, a Putative Glycosyltransferase Gene Downstream of vimE, Alters Glycosylation and Activation of the Gingipains in Porphyromonas gingivalis W83. Infect. Immun. 73: 3971-3982 [Abstract] [Full Text]  
  • Vanterpool, E., Roy, F., Fletcher, H. M. (2004). The vimE Gene Downstream of vimA Is Independently Expressed and Is Involved in Modulating Proteolytic Activity in Porphyromonas gingivalis W83. Infect. Immun. 72: 5555-5564 [Abstract] [Full Text]  
  • Goulet, V., Britigan, B., Nakayama, K., Grenier, D. (2004). Cleavage of Human Transferrin by Porphyromonas gingivalis Gingipains Promotes Growth and Formation of Hydroxyl Radicals. Infect. Immun. 72: 4351-4356 [Abstract] [Full Text]  
  • Paramaesvaran, M., Nguyen, K.-A., Caldon, E., McDonald, J. A., Najdi, S., Gonzaga, G., Langley, D. B., DeCarlo, A., Crossley, M. J., Hunter, N., Collyer, C. A. (2003). Porphyrin-Mediated Cell Surface Heme Capture from Hemoglobin by Porphyromonas gingivalis. J. Bacteriol. 185: 2528-2537 [Abstract] [Full Text]  
  • Curtis, M. A., Aduse Opoku, J., Rangarajan, M., Gallagher, A., Sterne, J. A. C., Reid, C. R., Evans, H. E. A., Samuelsson, B. (2002). Attenuation of the Virulence of Porphyromonas gingivalis by Using a Specific Synthetic Kgp Protease Inhibitor. Infect. Immun. 70: 6968-6975 [Abstract] [Full Text]  
  • Olczak, T., Dixon, D. W., Genco, C. A. (2001). Binding Specificity of the Porphyromonas gingivalis Heme and Hemoglobin Receptor HmuR, Gingipain K, and Gingipain R1 for Heme, Porphyrins, and Metalloporphyrins. J. Bacteriol. 183: 5599-5608 [Abstract] [Full Text]  


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