Two substrate‐targeting sites in the Yersinia protein tyrosine phosphatase co‐operate to promote bacterial virulence

• Published in: Molecular microbiology Vol. 55; no. 5; pp. 1346 - 1356
• Main Authors: Ivanov, Maya I., Stuckey, Jeanne A., Schubert, Heidi L., Saper, Mark A., Bliska, James B.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Science Ltd 01.03.2005; Blackwell Science; Blackwell Publishing Ltd
• Subjects: Adaptor Proteins, Signal Transducing; Animals; Bacteria; Bacterial Outer Membrane Proteins; Bacteriology; Binding Sites; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; HeLa Cells; Humans; Mice; Mice, Inbred C57BL; Microbiology; Miscellaneous; Molecular biology; Protein Tyrosine Phosphatases - analysis; Protein Tyrosine Phosphatases - metabolism; Proteins; Virulence - genetics; Yersinia pseudotuberculosis - enzymology; Yersinia pseudotuberculosis - genetics; Yersinia pseudotuberculosis - pathogenicity; Yersinia pseudotuberculosis Infections - microbiology; Microbiology; Enzyme; Virulence; Yersinia; Phosphoric monoester hydrolases; Bacteria; Hydrolases; Esterases; Molecular targeting; Enterobacteriaceae; Protein-tyrosine-phosphatase

Summary YopH is a protein tyrosine phosphatase and an essential virulence determinant of the pathogenic bacterium Yersinia. Yersinia delivers YopH into infected host cells using a type III secretion mechanism. YopH dephosphorylates several focal adhesion proteins including p130Cas in human epithelia...