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Titolo:
Genetic analyses of proteolysis, hemoglobin finding, and hemagglutination of Porphyromonas gingivalis - Construction of mutants with a combination ofrgpA, rgpB, kgp, and hagA
Autore:
Shi, Y; Ratnayake, DB; Okamoto, K; Abe, N; Yamamoto, K; Nakayama, K;
Indirizzi:
Kyushu Univ, Fac Dent, Dept Microbiol, Higashi Ku, Fukuoka 8128582, Japan Kyushu Univ Fukuoka Japan 8128582 ol, Higashi Ku, Fukuoka 8128582, Japan Kyushu Univ, Fac Dent, Dept Pharmacol, Fukuoka 8128582, Japan Kyushu UnivFukuoka Japan 8128582 Dept Pharmacol, Fukuoka 8128582, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 25, volume: 274, anno: 1999,
pagine: 17955 - 17960
SICI:
0021-9258(19990618)274:25<17955:GAOPHF>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEINASE LYS-GINGIPAIN; CYSTEINE PROTEINASE; ARG-GINGIPAIN; BACTEROIDES-GINGIVALIS; STRUCTURAL CHARACTERIZATION; MOLECULAR-CLONING; SEQUENCE-ANALYSIS; EPITHELIAL-CELLS; BINDING PROTEIN; ENCODING GENES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Nakayama, K KyushuJapan, Fac Dent, Dept Microbiol, Higashi Ku, 3-1-1, Fukuoka 8128582, Kyushu Univ 3-1-1 Fukuoka Japan 8128582 1-1, Fukuoka 8128582,
Citazione:
Y. Shi et al., "Genetic analyses of proteolysis, hemoglobin finding, and hemagglutination of Porphyromonas gingivalis - Construction of mutants with a combination ofrgpA, rgpB, kgp, and hagA", J BIOL CHEM, 274(25), 1999, pp. 17955-17960

Abstract

Porphyromonas gingivalis produces arginine-specific cysteine proteinase (Arg-gingipain, RGP) and lysine-specific cysteine proteinase (Lys-gingipain, KGP) in the extracellular and cell-associated forms. Two separate genes (rgpA and rgpB) and a single gene (kgp) have been found to encode RGP and KGP,respectively. We constructed rgpA rgpB kgp triple mutants by homologous recombination with cloned rgp and kgp DNA interrupted by drug resistance genemarkers. The triple mutants showed no RGP or KGP activity in either cell extracts or culture supernatants. The culture supernatants of the triple mutants grown in a rich medium had no proteolytic activity toward bovine serumalbumin or gelatin derived from human type I collagen. Moreover, the mutants did not grow in a defined medium containing bovine serum albumin as the sole carbon/energy source. These results indicate that the proteolytic activity of P, gingivalis toward bovine serum albumin and gelatin derived from human type I collagen appears to be attributable to RGP and KGP. The hemagglutinin gene hagA of P. gingivalis possesses the adhesin domain regions responsible for hemagglutination and hemoglobin binding that are also located in the C-terminal ;regions of rgpA and kgp. A rgpA kgp hagA triple mutant constructed in this study exhibited no hemagglutination using sheep erythrocytes or hemoglobin binding activity, as determined by a solid-phase bindingassay with horseradish peroxidase-conjugated human hemoglobin, indicating that the adhesin domains seem to be particularly important for P. gingivalis cells to agglutinate erythrocytes and bind hemoglobin, leading to heme acquisition.

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Documento generato il 01/12/20 alle ore 06:07:29