| Project/Area Number |
17591912
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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 |
Morphological basic dentistry
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| Research Institution | HIROSHIMA UNIVERSITY |
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Principal Investigator |
SUGAI Motoyuki Hiroshima University, Graduate School of Biomedical Sciences, Professor, 大学院医歯薬学総合研究科, 教授 (10201568)
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| Co-Investigator(Kenkyū-buntansha) |
KOMATSUZAWA Hitoshi Hiroshima University, Graduate School of Biomedical Sciences, Associate Professor, 大学院医歯薬学総合研究科, 助教授 (90253088)
FUJIWARA Tamaki Hiroshima University, Graduate School of Biomedical Sciences, Research Associate, 大学院医歯薬学総合研究科, 助手 (90274092)
OHARA Masaru Hiroshima University, Graduate School of Biomedical Sciences, Research Associate, 大学院医歯薬学総合研究科, 助手 (80253095)
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| Project Period (FY) |
2005 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2006: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2005: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | Periodontopathogenic / Cdt / Cytolethal Distending Toxin / antimicrobial peptide / defensin / A.actinomycetemcomitans / CDT / Omp / 歯周病細菌 / 細胞膨化壊死毒素 |
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| Research Abstract |
Study on A. actinomycetemcomitans Cytolethal Distending Toxin (CDT) : CDT is a protein toxin composed of three subunit, CdtA, CdtB and CdtC. A. actinommycetemcomitans CdtA posseses lipobox, consensus domain for lipid modification in its C-terminal. We demonstrated that 16^<th> cys in A. actinommycetemcomitans CdtA expressed in E. coli was modified with tritiated palmitate or glycerol. Posttranscriptional prosesing of the CdtA is inhibited by globomycin, a specific inhibitor for signal peptidase II, signal peptidase for lipoprotein. We also demonstrated that the CdtA expressed in E. coli is further processed at its N-terminal in periplasmic space and is converted to CdtA'. Furthermore, we showed that lipid-modification of CdtA is important for the secretion of Cdt complex (holotoxin) into culture media. We also demonstrated that there is a SNP in cdtB coding sequences. Hence, 281th amino acid of CdtB derived from clinically isolated A. actinomycetemcomitans is either H or R. Bioassay wi
… More
th mutated CdtB by site-directed mutagenesis indicated that positively charged amino acid at 281 is critical for Cdt activity.
Study on A. actinomycetemcomitans outer membrane protein: We have previously demonstrated that A. actinomycetemcomitans posseses several outer membrane proteins (Omp) and Omp100 has pleiotropic biological activities. We identified Omp100 as a major bacterial component inducing production of antimicrobial peptides from human gingival epidermal cells. Inhibitor assay strongy suggested that signaling pathway for hBD2 production is not by NF-kB pathway but by MAP-kinase pathway. Omp100 induces hBD2 production through associating with fibronectin and by way of integrin alpha5betal pathway. Cytokine induced by attachment of bacteria to epidermal cells also induces hBD2 expression.
Study on inducibility of antimicrobial peptides by periodontopathogenic bacteria. By using synthtic peptides, we evaluated susceptibility of periodontopathogenic bacteria to antimicrobial peptides. Our data indicated that LL37 and beta-defensin showed potent antimicrobial activity against periodontapathogenic bacteria. Less
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