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Titolo:
Unaltered expression of the major protease genes in a non-virulent recA-defective mutant of Porphyromonas gingivalis W83
Autore:
Abaibou, H; Ma, Q; Olango, GJ; Potempa, J; Travis, J; Fletcher, HM;
Indirizzi:
Loma Linda Univ, Dept Microbiol & Mol Genet, Loma Linda, CA 92350 USA LomaLinda Univ Loma Linda CA USA 92350 l Genet, Loma Linda, CA 92350 USA Jagiellonian Univ, Inst Mol Genet, Dept Microbiol & Immunol, Krakow, Poland Jagiellonian Univ Krakow Poland ept Microbiol & Immunol, Krakow, Poland Univ Georgia, Dept Biochem, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 rgia, Dept Biochem, Athens, GA 30602 USA
Titolo Testata:
ORAL MICROBIOLOGY AND IMMUNOLOGY
fascicolo: 1, volume: 15, anno: 2000,
pagine: 40 - 47
SICI:
0902-0055(200002)15:1<40:UEOTMP>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYSTEINE PROTEINASE; ARG-GINGIPAIN; LYS-GINGIPAIN; INVOLVEMENT; NITROCELLULOSE; COLONIZATION; COMPLEXES; W50;
Keywords:
Porphyromonas gingivalis; gene expression; protease; mutant; recA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Fletcher, HM Loma Linda Univ, Dept Microbiol & Mol Genet, Loma Linda, CA 92350 USA Loma Linda Univ Loma Linda CA USA 92350 Linda, CA 92350 USA
Citazione:
H. Abaibou et al., "Unaltered expression of the major protease genes in a non-virulent recA-defective mutant of Porphyromonas gingivalis W83", ORAL MICROB, 15(1), 2000, pp. 40-47

Abstract

Porphyromonas gingivalis FLL32, a recA mutant, was isolated during construction of a recA defective mutant of P. gingivalis W83 by allelic exchange mutagenesis. In contrast to W83 and FLL33, the typical recA(-) mutant previously reported, FLL32 was non-pigmented, lacked beta-hemolytic activity an blood agar and produced significantly less proteolytic activity. The proteolytic activity in FLL32 was mostly soluble. Expression of the rgpA, rgpB andkgp protease genes was unaltered in FLL32 when compared to FLL33 and the wild-type strain. FLL32 exhibited reduced virulence in a murine model and partially protected the animals immunized with that strain against a subsequent lethal challenge by the wild-type strain. These results indicate that the reduced level of proteolytic activity in FLL32 may be due to a defect in the processing of the proteases. Further, immunization with a non-virulent recA defective mutant of P. gingivalis can partially protect against a lethal wild-type challenge. The results from this study suggest that the recA locus may be involved in expression and regulation of proteolytic activity in P. gingivalis.

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Documento generato il 22/09/20 alle ore 07:05:31