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Por Secretion System-Dependent Secretion and Glycosylation of Porphyromonas gingivalis Hemin-Binding Protein 35
TLDR
Immunoblot analysis of P. gingivalis mutants deficient in the PorSS or in the biosynthesis of anionic polysaccharide-lipopolysaccharid (A-LPS) revealed that HBP35 is translocated to the cell surface via the Por SS, and glycosylation of CTD proteins occurs after removal of the CTD region. Expand
Arg-gingipain Acts as a Major Processing Enzyme for Various Cell Surface Proteins in Porphyromonas gingivalis*
TLDR
Evidence that RGP acts as a major processing enzyme for various cell surface and secretory proteins in P. gingivalis is provided and Lys-gingipain was found to be abnormally processed in the RGP-null mutant, suggesting that KGP is not involved in the normal processing mechanisms of these proteins. Expand
Haemoglobin receptor protein is intragenically encoded by the cysteine proteinase‐encoding genes and the haemagglutinin‐encoding gene of Porphyromonas gingivalis
TLDR
Results strongly indicate a close relationship among HGP15 production, haemoglobin adsorption and haem accumulation of P. gingivalis. Expand
Purification and characterization of a novel arginine-specific cysteine proteinase (argingipain) involved in the pathogenesis of periodontal disease from the culture supernatant of Porphyromonas
TLDR
Results suggests that argingipain plays a key role as a major virulence factor from P. gingivalis in the development of periodontal disease via the direct destruction ofperiodontal tissue components and the disruption of normal host defense mechanisms. Expand
Involvement of arginine-specific cysteine proteinase (Arg-gingipain) in fimbriation of Porphyromonas gingivalis.
TLDR
Investigation of the role of RGP in the formation of P. gingivalis fimbriae suggests that RGP may function as a processing proteinase for fimbrilin maturation. Expand
Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: cell surface polysaccharide as an anchorage for gingipains.
TLDR
Results indicate that porR is involved in biosynthesis of cell surface polysaccharide that may function as an anchorage for Rgp, Kgp, haemagglutinins and the haemoglobin receptor protein. Expand
Suppression of Pathogenicity of Porphyromonas gingivalis by Newly Developed Gingipain Inhibitors
TLDR
Results indicate that the newly developed KYT-1 andKYT-36 both should provide a broader application in studies of this important class of enzymes and facilitate the development of new approaches to periodontal diseases. Expand
A two-component system regulates gene expression of the type IX secretion component proteins via an ECF sigma factor
TLDR
The results demonstrate that PorX and PorY act as a response regulator and a histidine kinase, respectively, of a two component system (TCS), although they are separately encoded on the chromosome. Expand
Role for Gingipains in Porphyromonas gingivalis Traffic to Phagolysosomes and Survival in Human Aortic Endothelial Cells
TLDR
It is found that the number of intracellular viable WT cells decreased more slowly than that of KDP136 cells, thus suggesting that gingipains contribute to bacterial survival, but not to trafficking, within the infected cells. Expand
Construction and Characterization of Arginine-specific Cysteine Proteinase (Arg-gingipain)-deficient Mutants of Porphyromonas gingivalis
TLDR
It is demonstrated that Arg-gingipain makes a significant contribution to the virulence of P. gingivalis, and a major part of the hemagglutinin activity of the organism is associated with the two genes. Expand
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