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The Journal of Biochemistry
Year: 2010  |  Volume: 147  |  Issue: 3  |  Page No.: 317 - 325

Neutralization of toxic haem by Porphyromonas gingivalis haemoglobin receptor

N. T. T Nhien, N. T Huy, M Naito, T Oida, D. T Uyen, M Huang, M Kikuchi, S Harada, K Nakayama, K Hirayama and K. Kamei    

Abstract:

Free haem 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 haem as an iron nutrient source for P. gingivalis. Using erythrocyte and its membrane as a model, results from the present study demonstrate that recombinant HbR expressed in Escherichia coli could inhibit haem-induced haemolysis, probably through removing haem from the haem–membrane complex and lowering free haem toxicity by mediating dimerization of haem molecules. The ability to protect a cell membrane from haem toxicity is a new function for HbR.

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