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Titolo:
VIRULENCE OF A PORPHYROMONAS-GINGIVALIS W83 MUTANT DEFECTIVE IN THE PRTH GENE
Autore:
FLETCHER HM; SCHENKEIN HA; MORGAN RM; BAILEY KA; BERRY CR; MACRINA FL;
Indirizzi:
VIRGINIA COMMONWEALTH UNIV,DEPT MICROBIOL & IMMUNOL RICHMOND VA 23298 VIRGINIA COMMONWEALTH UNIV,CLIN RES CTR PERIODONTAL DIS RICHMOND VA 23298
Titolo Testata:
Infection and immunity
fascicolo: 4, volume: 63, anno: 1995,
pagine: 1521 - 1528
SICI:
0019-9567(1995)63:4<1521:VOAPWM>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
BLACK-PIGMENTED BACTEROIDES; ANTIBIOTIC-RESISTANCE; COLLAGENASE ACTIVITY; ESCHERICHIA-COLI; PROTEASE GENE; SEQUENCE; W50; STRAINS; PHAGOCYTOSIS; CLINDAMYCIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
H.M. Fletcher et al., "VIRULENCE OF A PORPHYROMONAS-GINGIVALIS W83 MUTANT DEFECTIVE IN THE PRTH GENE", Infection and immunity, 63(4), 1995, pp. 1521-1528

Abstract

In a previous study we cloned and determined the nucleotide sequence of the prtH gene from Porphyromonas gingivalis W83. This gene specifies a 97-kDa protease which is normally found in the membrane vesicles produced by P. gingivalis and which cleaves the C3 complement protein under defined conditions. We developed a novel ermF-ermAM antibiotic resistance gene cassette, which was used with the cloned prtH gene to prepare an insertionally inactivated allele of this gene. This genetic construct was introduced by electroporation into P. gingivalis W83 in order to create a protease-deficient mutant by recombinational allelic exchange. The mutant strain, designated V2296, was compared with the parent strain W83 for proteolytic activity and virulence. Extracellularprotein preparations from V2296 showed decreased proteolytic activitycompared with preparations from W83. Casein substrate zymography revealed that the 97-kDa proteolytic component as well as a 45-kDa protease was missing in the mutant, In in vivo experiments using a mouse model, V2296 was dramatically reduced in virulence compared with the wild-type W83 strain. A molecular survey of several clinical isolates of P.gingivalis using the prtH gene as a probe suggested that prtH gene sequences were conserved and that they may have been present in multiplecopies. Two of 10 isolates did not hybridize with the prtH gene probe, These strains, like the V2296 mutant, also displayed decreased virulence in the mouse model. Taken together, these results suggest an important role for P. gingivalis proteases in soft tissue infections and specifically indicate that the prtH gene product is a virulence factor.

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Documento generato il 01/12/20 alle ore 07:29:50