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Titolo:
ADHERENCE OF PORPHYROMONAS-GINGIVALIS TO MATRIX PROTEINS VIA A FIMBRIAL CRYPTIC RECEPTOR EXPOSED BY ITS OWN ARGININE-SPECIFIC PROTEASE
Autore:
KONTANI M; KIMURA S; NAKAGAWA I; HAMADA S;
Indirizzi:
OSAKA UNIV,FAC DENT,DEPT ORAL MICROBIOL SUITA OSAKA 565 JAPAN OSAKA UNIV,FAC DENT,DEPT ORAL MICROBIOL SUITA OSAKA 565 JAPAN
Titolo Testata:
Molecular microbiology
fascicolo: 6, volume: 24, anno: 1997,
pagine: 1179 - 1187
SICI:
0950-382X(1997)24:6<1179:AOPTMP>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
SURFACE-PLASMON RESONANCE; BIOSPECIFIC INTERACTION ANALYSIS; BLACK-PIGMENTED BACTEROIDES; TRYPSIN-LIKE ACTIVITY; KINETIC-PARAMETERS; ARG-GINGIPAIN; BIOSENSOR; BINDING; MICROORGANISMS; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
M. Kontani et al., "ADHERENCE OF PORPHYROMONAS-GINGIVALIS TO MATRIX PROTEINS VIA A FIMBRIAL CRYPTIC RECEPTOR EXPOSED BY ITS OWN ARGININE-SPECIFIC PROTEASE", Molecular microbiology, 24(6), 1997, pp. 1179-1187

Abstract

Porphyromonas gingivalis, a Gram-negative anaerobe, is known to be involved in the pathogenesis of periodontitis. P. gingivalis fimbriae, which are proteinaceous appendages extending from the cell surface, maycontribute to the adherence of the organism to the host cell surface. We previously suggested that arginine-specific protease produced by P. gingivalis enhanced the adherence of purified fimbriae to fibroblasts or matrix proteins. In this study, we have revealed the mechanism ofthe enhanced binding of fimbriae by the protease in more detail. Arg-specific protease and fimbriae were obtained from P. gingivalis 381 cells and purified, We then analysed the interaction of fimbriae and immobilized fibronectins (intact or partially degraded fibronectin by thepurified protease) by using the real-time biomolecular interaction analysis (BIAcore) system with an optical biosensor based on the principles of surface plasmon resonance. BIAcore profiles demonstrated an enhanced interaction between fimbriae and protease-degraded fibronectin, We also showed specific binding of fimbriae to the degraded fibronectin by means of BIAcore analysis, The binding of biotinylated fimbriae to immobilized fibronectin was examined by enzyme-linked biotin-avidin assay. The purified protease enhanced the fimbrial binding to the immobilized fibronectin. The enhancement was inhibited by the addition of L-Arg, or oligopeptides containing the Arg residue at the C-terminus in the fimbrial binding reaction, suggesting that the P. gingivalis fimbriae may potentially have an ability to bind tightly to the Arg residue at C-terminus. Taken together, these studies indicate that P. gingivalis arginine-specific protease can expose a cryptitope in the matrixprotein molecules, i.e. the C-terminal Arg residue of the host matrixproteins, so that the organism can adhere to the surface layer in theoral cavity through fimbriae-Arg interaction (a novel host-parasite relationship).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 21:46:50