| Project/Area Number |
14571766
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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 |
Functional basic dentistry
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| Research Institution | Nagasaki University |
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Principal Investigator |
KOBAYAKAWA Takeshi Nagasaki University, GRADUATE SCHOOL OF BIOMEDICAL SCIENCES, Research Fellow, 大学院・医歯薬学総合研究科, 教務職員 (10153587)
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| Co-Investigator(Kenkyū-buntansha) |
ONO Toshio Nagasaki University, GRADUATE SCHOOL OF BIOMEDICAL SCIENCES, Instructor, 大学院・医歯薬学総合研究科, 助手 (80050607)
NAKAYAMA Koji Nagasaki University, GRADUATE SCHOOL OF BIOMEDICAL SCIENCES, Professor, 大学院・医歯薬学総合研究科, 教授 (80150473)
NEMOTO Takayuki Nagasaki University, GRADUATE SCHOOL OF BIOMEDICAL SCIENCES, Professor, 大学院・医歯薬学総合研究科, 教授 (90164665)
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| Project Period (FY) |
2002 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥2,800,000 (Direct Cost: ¥2,800,000)
Fiscal Year 2003: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 2002: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | HtpG / HSP90 / molecular chaperone / P. gingivalis / periodontitis / stress |
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| Research Abstract |
Periodontal disease is a chronic infectious disease, with PF gingivalis, being most implicated pathogens. In the present study, we investigated the role of PF gingivalis HtpG (PgHtpG), a bacterial homologue of mammalian Hsp90 on the growth of PF gingivalis and also accessed the immunological cross-reactivity of anti-PgHtpG antibody against the members of the Hsp90 family from various species. The HtpG gene disruption didn't affect its survival, but altered the _sensitivity under stress conditions, such as elevated temperature, the presence of H_2O_2 or ethanol. Immunological analysis indicated that mammalian Hsp90 shared some of the immunological reactivity with yeast Hsc82, human Grp94, and human Trap1. Taken together, tin infectious diseases such as periodontitis, the antibodies produced against HtpG of infected bacteria are not likely to induce autoimmune responses.
And we investigated the important amino acid residues related to the dimer structure of Hsp90 isoform using bacterial two-hybrid system. The, formation of the Hsp90 dimer was related to the amino acid residue mutations in MIDDLE domain between a and fi -isoform, and described the importance of this region.
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