A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant.

作者: Edouard E. Galyov , Sebastian Håkansson , Åke Forsberg , Hans Wolf-Watz

DOI: 10.1038/361730A0

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摘要: PHOSPHORYLATION of proteins catalysed by protein kinases is associated with central functions in growth and proliferation the eukaryotic cell, are particularly important signal transduction pathways1,2. Enterobacterial structurally functionally different from kinases3,4, no prokaryotic kinase has so far been described implicating a direct role for this activity virulence. Virulent Yersinia possess common virulence plasmid that encodes number secreted (Yops)5–7, which YopH protein-tyrosine phosphatase key function block phagocytosis pathogen8–10. Here we report pseudotuberculosis (YpkA) extensive homology to Ser/Thr kinases3,11. Specific mutants ypkA resulted avirulent strains. Thus, YpkA is, our knowledge, first reported involved pathogenicity, presumably interfering pathways target cell.

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