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Pathogenic Yersinia species evade host immune systems through the injection of Yersinia outer proteins (Yops) into phagocytic cells. One Yop, YopO, also known as YpkA, induces actin-filament disruption, impairing phagocytosis. Here we describe the X-ray structure of Yersinia enterocolitica YopO in complex with actin, which reveals that YopO binds to an actin monomer in a manner that blocks polymerization yet allows the bound actin to interact with host actin-regulating proteins. SILAC-MS and biochemical analyses confirm that actin-polymerization regulators such as VASP, EVL, WASP, gelsolin and the formin diaphanous 1 are directly sequestered and phosphorylated by YopO through formation of ternary complexes with actin. This leads to a model in which YopO at the membrane sequesters actin from polymerization while using the bound actin as bait to recruit, phosphorylate and misregulate host actin-regulating proteins to disrupt phagocytosis.

Original publication

DOI

10.1038/nsmb.2964

Type

Journal article

Journal

Nat Struct Mol Biol

Publication Date

03/2015

Volume

22

Pages

248 - 255

Keywords

Actins, Bacterial Outer Membrane Proteins, Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Models, Molecular, Phagocytosis, Phosphorylation, Polymerization, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Yersinia enterocolitica