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Titolo:
HEMOGLOBIN RECEPTOR PROTEIN IS INTRAGENICALLY ENCODED BY THE CYSTEINEPROTEINASE-ENCODING GENES AND THE HEMAGGLUTININ-ENCODING GENE OF PORPHYROMONAS-GINGIVALIS
Autore:
NAKAYAMA K; RATNAYAKE DB; TSUKUBA T; KADOWAKI T; YAMAMOTO K; FUJIMURA S;
Indirizzi:
KYUSHU UNIV,FAC DENT,DEPT MICROBIOL FUKUOKA 812 JAPAN KYUSHU UNIV,FAC DENT,DEPT PHARMACOL FUKUOKA 812 JAPAN MATSUMOTO DENT COLL,DEPT ORAL MICROBIOL SHIOJIRI 39907 JAPAN
Titolo Testata:
Molecular microbiology
fascicolo: 1, volume: 27, anno: 1998,
pagine: 51 - 61
SICI:
0950-382X(1998)27:1<51:HRPIIE>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACTEROIDES-GINGIVALIS; ARG-GINGIPAIN; HEMOGLOBIN RECEPTOR; BINDING PROTEINS; HEMAGGLUTININ; IRON; CLONING; W50; VIRULENCE; ERYTHROCYTES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
K. Nakayama et al., "HEMOGLOBIN RECEPTOR PROTEIN IS INTRAGENICALLY ENCODED BY THE CYSTEINEPROTEINASE-ENCODING GENES AND THE HEMAGGLUTININ-ENCODING GENE OF PORPHYROMONAS-GINGIVALIS", Molecular microbiology, 27(1), 1998, pp. 51-61

Abstract

The obligately anaerobic bacterium Porphyromonas gingivalis produces characteristic black-pigmented colonies on blood agar. It is thought that the black pigmentation is caused by haem accumulation and is related to virulence of the microorganism. P. gingivalis cells expressed a prominent 19 kDa protein when grown on blood agar plates. Analysis of its N-terminal amino acid sequence indicated that the 19 kDa protein was encoded by an internal region (HGP15 domain) of an arginine-specific cysteine proteinase (Arg-gingipain, RGP)-encoding gene (rgp1) and was also present in genes for lysine-specific cysteine proteinases (prtPand kgp) and a haemagglutinin (hagA) of P. gingivalis. The HGP15 domain protein was purified from an HGP15-overproducing Escherichia coli and was found to have the ability to bind to haemoglobin in a pH-dependent manner. The anti-HGP15 antiserum reacted with the 19 kDa haemoglobin-binding protein in the envelope of P. gingivalis. P. gingivalis wild-type strain showed pH-dependent haemoglobin adsorption, whereas its non-pigmented mutants that produced no HGP15-related proteins showed deficiency in haemoglobin adsorption. These results strongly indicate aclose relationship among HGP15 production, haemoglobin adsorption andhaem accumulation of P. gingivalis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 16:04:39