Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
TRYPSIN-LIKE PROTEASE ACTIVITY OF PORPHYROMONAS-GINGIVALIS AS A POTENTIAL VIRULENCE FACTOR IN A MURINE LESION MODEL
Autore:
KESAVALU L; HOLT SC; EBERSOLE JL;
Indirizzi:
UNIV TEXAS,HLTH SCI CTR,SCH DENT,DEPT PERIODONT,7703 FLOYD CURL DR SAN ANTONIO TX 78284 UNIV TEXAS,HLTH SCI CTR,SCH DENT,DEPT PERIODONT SAN ANTONIO TX 78284 UNIV TEXAS,HLTH SCI CTR,DEPT MICROBIOL SAN ANTONIO TX 78284
Titolo Testata:
Microbial pathogenesis
fascicolo: 1, volume: 20, anno: 1996,
pagine: 1 - 10
SICI:
0882-4010(1996)20:1<1:TPAOPA>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
BLACK-PIGMENTED BACTEROIDES; EXTRACELLULAR MEMBRANE-VESICLES; HUMAN DENTAL PLAQUE; W50; ENZYME; STRAINS; MICE; IMMUNIZATION; DEGRADATION; INFECTION;
Keywords:
PROTEASES; P-GINGIVALIS; VIRULENCE; MURINE MODEL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
L. Kesavalu et al., "TRYPSIN-LIKE PROTEASE ACTIVITY OF PORPHYROMONAS-GINGIVALIS AS A POTENTIAL VIRULENCE FACTOR IN A MURINE LESION MODEL", Microbial pathogenesis, 20(1), 1996, pp. 1-10

Abstract

Porphyromonas gingivalis possesses a large number of enzymatic activities which might be important in the virulence of this putative periodontopathogen. The purpose of this study was to examine these enzymaticactivities in vivo in a murine model to assess their role in soft tissue destruction. Whole cells of P. gingivalis strains whether grown onblood agar plates or in broth exhibited high levels of alkaline phosphatase (ALPase), a trypsinlike protease (TLPase), acid phosphatase (ACPase), N-acetyl beta-glucosaminidase (Na beta-Gase) enzymes and collagenolytic activities. P. gingivalis W50 treated with 2 mM Na-P-tosyl-L-lysine chloromethyl ketone (TLCK)/phenylmethylsulfonyl fluoride (PMSF)prior to subcutaneous infection of mice failed to induce a phlegmonous abscess and lethality characteristic of animals challenged with untreated P. gingivalis. Comparison of wild type P. gingivalis strain 3079.03 with its protease-deficient (TLPase-negative) mutant NG4B19 revealed the mutant to be avirulent (no lesion and no death) in this model. P. gingivalis BEI and SW5 mutants (parent W50), which partially lackedTLPase enzyme activity produced only localized lesions, and no death. Thus, the TLPase enzyme appears to be correlated with the lesion type(spreading or localized), lesion size, and death in this mouse abscess model. Therefore, the enzymatic activities of P. gingivalis and specifically the TLPase enzyme could play an important role in periodontaldisease by enhancing bacterial spread and degrading gingival tissues. (C) 1996 Academic Press Limited.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 00:43:44