Irp9, Encoded by the High-Pathogenicity Island of Yersinia enterocolitica, Is Able To Convert Chorismate into Salicylate, the Precursor of the Siderophore Yersiniabactin

AUTOR(ES)

Pelludat, Cosima

FONTE

American Society for Microbiology

RESUMO

The Irp9 protein of Yersinia enterocolitica participates in the synthesis of salicylate, the precursor of the siderophore yersiniabactin. In Pseudomonas species, salicylate synthesis is mediated by two enzymes: isochorismate synthase and isochorismate pyruvate-lyase. Both enzymes are required for complementation of a Yersinia irp9 mutant. However, irp9 is not able to complement Escherichia coli entC for the production of enterobactin, which requires isochorismate as a precursor. These results suggest that Irp9 directly converts chorismate into salicylate.

Documentos Relacionados

• Common and Specific Characteristics of the High-Pathogenicity Island of Yersinia enterocolitica
• Analysis of the Corynebacterium diphtheriae DtxR Regulon: Identification of a Putative Siderophore Synthesis and Transport System That Is Similar to the Yersinia High-Pathogenicity Island-Encoded Yersiniabactin Synthesis and Uptake System
• Novel Virulence-Associated Type II Secretion System Unique to High-Pathogenicity Yersinia enterocolitica
• Yersinia High-Pathogenicity Island Contributes to Virulence in Escherichia coli Causing Extraintestinal Infections
• Transfer of the Core Region Genes of the Yersinia enterocolitica WA-C Serotype O:8 High-Pathogenicity Island to Y. enterocolitica MRS40, a Strain with Low Levels of Pathogenicity, Confers a Yersiniabactin Biosynthesis Phenotype and Enhanced Mouse Virulence