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Titolo:
ARG-GINGIPAIN ACTS AS A MAJOR PROCESSING ENZYME FOR VARIOUS CELL-SURFACE PROTEINS IN PORPHYROMONAS-GINGIVALIS
Autore:
KADOWAKI T; NAKAYAMA K; YOSHIMURA F; OKAMOTO K; ABE N; YAMAMOTO K;
Indirizzi:
KYUSHU UNIV,FAC DENT,DEPT PHARMACOL,HIGASHI KU FUKUOKA 8128582 JAPAN KYUSHU UNIV,FAC DENT,DEPT PHARMACOL,HIGASHI KU FUKUOKA 8128582 JAPAN KYUSHU UNIV,FAC DENT,DEPT MICROBIOL,HIGASHI KU FUKUOKA 8128582 JAPAN AICHI GAKUIN UNIV,SCH DENT,DEPT MICROBIOL NAGOYA AICHI 4648650 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 44, volume: 273, anno: 1998,
pagine: 29072 - 29076
SICI:
0021-9258(1998)273:44<29072:AAAAMP>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANAEROBE BACTEROIDES-GINGIVALIS; TRYPSIN-LIKE PROTEASE; CYSTEINE PROTEINASE; MOLECULAR-CLONING; PERIODONTAL-DISEASE; STRUCTURAL CHARACTERIZATION; POSSIBLE INVOLVEMENT; LYS-GINGIPAIN; GENE PRTR; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
T. Kadowaki et al., "ARG-GINGIPAIN ACTS AS A MAJOR PROCESSING ENZYME FOR VARIOUS CELL-SURFACE PROTEINS IN PORPHYROMONAS-GINGIVALIS", The Journal of biological chemistry, 273(44), 1998, pp. 29072-29076

Abstract

Arg-gingipain (RGP) is an Arg-X-specific cysteine proteinase producedby the Gram-negative anaerobe Porphyromonas gingivalis and has been shown to be a potent virulence factor in progressive periodontal disease (Nakayama, K., Kadowaki, T,, Okamoto, K,, and Yamamoto, K, (1995) J,Biol, Chem, 270, 23619-23626), In this study, we provide evidence that RGP acts as a major processing enzyme for various cell surface and secretory proteins in P, gingivalis. Fimbrilin, a major component of fimbriae, remained in the precursor form in the RGP-null mutant. Prefimbrilin expressed in Escherichia coil was converted to the mature fimbrilin in vitro when incubated with purified RGP, but its conversion was suppressed by potent RGP inhibitors. The results were consistent with the electron microscopic observation indicating little or no fimbriation in the RGP-null mutant. The immunogenic 75-kDa cell surface proteinwas also shown to retain its preform in the RGP-null mutant. In addition, Lys-gingipain (KGP) was found to be abnormally processed in the RGP-null mutant, In contrast, both prefimbrilin and the 75-kDa protein precursor were processed to their respective mature forms in the KG;P-null mutant, suggesting that KGP is not involved in the normal processing mechanisms of these proteins. These results suggest that RGP not only acts as a direct virulence factor but also makes a significant contribution as a major processing enzyme to the virulence of P. gingivalis,

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Documento generato il 05/12/20 alle ore 00:43:56