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Urease is not involved in the virulence of Yersinia pseudotuberculosis in mice.

ABSTRACT: A chromosomal locus (ure) involved in the production of urease activity in the bacterial pathogen Yersinia pseudotuberculosis was characterized. The genetic organization of the Y. pseudotuberculosis ure locus closely resembles that of the related ureolytic Yersinia species Y. enterocolitica. This locus encompasses seven open reading frames encoding polypeptides with predicted molecular weights of 10,894 (UreA), 15,820 (UreB), 61,001 (UreC), 25,801 (UreE), 24,551 (UreF), 20,330 (UreG), and 31,308 (UreD). The polypeptides have 85 to 96% identity with the corresponding Ure polypeptides of Y. enterocolitica serotype 0:8. Restriction fragment length polymorphisms of the ure loci from 12 unrelated Y. pseudotuberculosis strains produced by HaeIII and MboI indicate a low level of genetic variability of this locus in this species. The role of urease in the pathogenicity of Y. pseudotuberculosis was studied by constructing an isogenic urease-negative mutant obtained by disruption of structural gene ureB by aphA-3', which encodes kanamycin resistance. Experimental infection of mice with this mutant demonstrates that urease is not essential for Y. pseudotuberculosis virulence. Urease might be required mostly during the saprophytic life of this pathogen.

SUBMITTER: Riot B

PROVIDER: S-EPMC175258 | biostudies-other | 1997 May

REPOSITORIES: biostudies-other

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Urease is not involved in the virulence of Yersinia pseudotuberculosis in mice.

Riot B B Berche P P Simonet M M

Infection and immunity 19970501 5

A chromosomal locus (ure) involved in the production of urease activity in the bacterial pathogen Yersinia pseudotuberculosis was characterized. The genetic organization of the Y. pseudotuberculosis ure locus closely resembles that of the related ureolytic Yersinia species Y. enterocolitica. This locus encompasses seven open reading frames encoding polypeptides with predicted molecular weights of 10,894 (UreA), 15,820 (UreB), 61,001 (UreC), 25,801 (UreE), 24,551 (UreF), 20,330 (UreG), and 31,308 ...[more]

PMID: 9125594

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Project description:Although bacterial peptidases are known to be produced by various microorganisms, including pathogenic bacteria, their role in bacterial physiology is not fully understood. In particular, oligopeptidases are thought to be mainly involved in degradation of short peptides e.g. leader peptides released during classical protein secretion pathways. The aim of this study was to investigate effects of inactivation of an oligopeptidase encoding gene opdA gene of Yersinia pseudotuberculosis on bacterial properties in vivo and in vitro, and to test dependence of the enzymatic activity of the respective purified enzyme on the presence of different divalent cations.In this study we found that oligopeptidase OpdA of Yersinia pseudotuberculosis is required for bacterial virulence, whilst knocking out the respective gene did not have any effect on bacterial viability or growth rate in vitro. In addition, we studied enzymatic properties of this enzyme after expression and purification from E. coli. Using an enzyme depleted of contaminant divalent cations and different types of fluorescently labelled substrates, we found strong dependence of its activity on the presence of particular cations. Unexpectedly, Zn2+ showed stimulatory activity only at low concentrations, but inhibited the enzyme at higher concentrations. In contrast, Co2+, Ca2+ and Mn2+ stimulated activity at all concentrations tested, whilst Mg2+ revealed no effect on the enzyme activity at all concentrations used.The results of this study provide valuable contribution to the investigation of bacterial peptidases in general, and that of metallo-oligopeptidases in particular. This is the first study demonstrating that opdA in Yersinia pseudotuberculsosis is required for pathogenicity. The data reported are important for better understanding of the role of OpdA-like enzymes in pathogenesis in bacterial infections. Characterisation of this protein may serve as a basis for the development of novel antibacterials based on specific inhibition of this peptidase activity.

Dataset Information

Urease is not involved in the virulence of Yersinia pseudotuberculosis in mice.

Publications

Urease is not involved in the virulence of Yersinia pseudotuberculosis in mice.

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