A 35-kDa co-aggregation factor is a hemin binding protein in Porphyromonas gingivalis

It has been known that Porphyromonas gingivalis has an obligate requirement for hemin or selected heme- or Fe-containing compounds for its growth. In addition, the influence of hemin on the expression of several putative virulence factors produced by this bacterium has also been recently documented;...

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Published in:Biochemical and biophysical research communications 2003-01, Vol.300 (2), p.351-356
Main Authors: Shibata, Yasuko, Hiratsuka, Koichi, Hayakawa, Mitsuo, Shiroza, Teruaki, Takiguchi, Hisashi, Nagatsuka, Yasuko, Abiko, Yoshimitsu
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Outer Membrane Proteins - metabolism
Bacterial Outer Membrane Proteins - physiology
Base Sequence
Carrier Proteins - metabolism
Carrier Proteins - physiology
Hemeproteins - metabolism
Hemeproteins - physiology
Hemin - metabolism
Hemin binding
Molecular Sequence Data
P. gingivalis
Periodontal diseases
Porphyromonas gingivalis - pathogenicity
Protoporphyrins - metabolism
Virulence factors
Virulence Factors - metabolism
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Summary:It has been known that Porphyromonas gingivalis has an obligate requirement for hemin or selected heme- or Fe-containing compounds for its growth. In addition, the influence of hemin on the expression of several putative virulence factors produced by this bacterium has also been recently documented; however, the mechanisms involved in hemin uptake are poorly defined. We succeeded in cloning the gene coding for the 35-kDa protein, which was specifically expressed in P. gingivalis and seemed to confer colonizing activities. Recently, we have constructed the P. gingivalis 381 mutant defective in the 35-kDa protein by insertion mutagenesis. The beige mutant exhibited little co-aggregation and the virulence was also decreased. Based on these results and homology search analysis, we focused on assessing the hemin bindings and found the heme regulatory motif (HRM) as a hemin direct binding site. The 35-kDa protein did possess the binding ability of selected protoporphyrins involving the hemin. These results demonstrated that 35-kDa protein is one of the hemin binding proteins in P. gingivalis and suggested that hemin binding ability of 35-kDa protein is important for the expression of virulence in P. gingivalis.
ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(02)02826-7