Pathological analysis based molecular interaction of the attachement factors of periodontal pathogens
| Project/Area Number |
13671982
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
病態科学系歯学(含放射線系歯学)
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| Research Institution | Nihon University |
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Principal Investigator |
SHIBATA Yasuko Nihon University, School of Dentistry at Matsudo, Lecturer (Full-Time), 松戸歯学部, 講師 (90133438)
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| Project Period (FY) |
2001 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥2,300,000 (Direct Cost: ¥2,300,000)
Fiscal Year 2003: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 2002: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 2001: ¥1,000,000 (Direct Cost: ¥1,000,000)
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| Keywords | Porphyromonas gingivalis / hemagglutinin / hemin / Antigen-antibody binding / Periodontal diseases / redox / Thioredoxin / Xeno mouse / transchromo-mouse / 歯周病病原因子 / ヘミン結合活性 / ヒト型抗体 / 赤血球凝集活性 / インフルエンザ / ヘミン結合 / HBP35 / ヒト型モノクローナル抗体 / ゼノマウス |
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| Research Abstract |
The analysis based on the ligand interaction was carried out on erythrocyte aggregating factor (hemagglutinin) and coaggregation factor P. gingivalis mentioned as an attachment factor. First, it should be necessary the Motif/Block search of these molecules of P. gingivalis, thus the specific motif in the hemagglutinin or the coaggregation factor to collate the ligand binding were searched. The primary structure of hemagglutinin of P. gingivalis set against that of influenza virus, and the commonality of activity and structure was compared. It was found that amino acid stretch of functional site of the P. gingivalis hemagglutinin were also exsisting amino acid stretch in influenza virus. We also showed that the human type monoclonal antibodies against the hemagglutinin domain molecules from P. gingivalis inhibited the hemagglutination of influenza virus. Moreover, these antibodies also neutralized the influenza virus infection to cells in vitro. It was proven that there was a cross-reaction of antibodies against the both hemagglutinin molecules of P. gingivalis and influenza virus.
Molecular structure elucidation of the coaggregation factor that was related to the oral attachment was tried. The coaggregation factor of P. gingivalis was the multifunctional molecule. We demonstrated this protein was one of the hemin binding proteins. Considering survival of this bacterium and true role of the hemin binding protein, the following were shown : Oxidization reducibility of the hemin molecule and possibility of oxygen inclusion. In addition, it was proven that heme-binding structure of this protein may be based on the cysteine residue. Production of the recombinant proteins that converted the cysteine residues into the serine residues were used to clarify which cysteine residue was related the hemin binding. Interestingly, the active center of the thioredoxin had been made in the two inside, and the relation with the oxidoreduction mechanism was speculated.
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Report
(4 results)
Research Products
(23 results)
