| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Outline of Final Research Achievements |
Porphyromonas gingivalis possesses cysteine proteases named gingipains that act as important virulence factors. Gingipains, which consist of Arg-gingipain A (RgpA), Arg-gingipain B (RgpB) and Lys-gingipain (Kgp), have a characteristic Ig-like domain of the peptidase family C25 that is found at the C-terminal region of the protease domain in almost all family members. When introducing a plasmid encoding either gingipain lacking the common structure or gingipain with an incomplete common structure into a P. gingivalis gingipain-null (rgpA rgpB kgp) mutant, the mutant gingipains were not detected in the cells, whereas mutant gingipains with high molecular mass accumulated in the membrane fraction after introducing the plasmids into an rgpA rgpB kgp htrA mutant, indicating that housekeeping protease degrades the mutant gingipains.
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