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Journal of Biochemistry Advance Access published online on October 27, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp164
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Neutralization of Toxic Heme by Porphyromonas gingivalis Hemoglobin Receptor

Nguyen Thanh Thuy Nhien1, Nguyen Tien Huy2, Mariko Naito3, Tatsuo Oida4, Dinh Thanh Uyen1,5, Mingguo Huang2, Mihoko Kikuchi2,6, Shigeharu Harada1, Koji Nakayama3, Kenji Hirayama2,6,* and Kaeko Kamei1,*

1 Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
2 Department of Immunogenetics, Institute of Tropical Medicine (NEKKEN), Nagasaki University, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan
3 Division of Microbiology and Oral Infection, Department of Molecular Microbiology and Immunology, Graduate School of Biomedical Sciences, Nagasaki University, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan
4 Department of Chemistry and Materials Technology, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
5 Venture Laboratory, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
6 Center for International Collaborative Research, Nagasaki University, 1-12-4 Sakamoto, Nagasaki

* Corresponding authors Kenji Hirayama, Kaeko Kamei. Mailing address: Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan, Tel: +81-75-724-7553, Fax: +81-75-724-7541. E-mail: kame{at}kit.ac.jp (K. Kamei) or hiraken{at}nagasaki-u.ac.jp (K. Hirayama)

Received September 21, 2009; Accepted October 9, 2009


  Abstract

Free heme is known to be toxic to organs, tissues and cells. It enhances permeability by binding to a cell membrane, which leads to cell death, and damages lipids, proteins and DNA through the generation of reactive oxygen species. Lysine- and arginine-specific gingipains (Kgp and RgpA/B) are major proteinases that play an important role in the pathogenicity of a black-pigmented periodontopathogen named Porphyromonas gingivalis. One of the adhesin domains of gingipain, HbR could bind heme as an iron nutrient source for Porphyromonas gingivalis. Using erythrocyte and its membrane as a model, results from the present study demonstrate that recombinant HbR expressed in Escherichia coli could inhibit heme-induced hemolysis, probably through removing heme from heme membrane complex and lowering free heme toxicity by mediating dimerization of heme molecules. The ability to protect a cell membrane from heme toxicity is a new function for HbR.

Key Words: gingipain, HbR, heme, membrane damage, Porphyromonas


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