4.8 Article

A Bacterial Effector Mimics a Host HSP90 Client to Undermine Immunity

Journal

CELL
Volume 179, Issue 1, Pages 205-+

Publisher

CELL PRESS
DOI: 10.1016/j.cell.2019.08.020

Keywords

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Funding

  1. Centre for Preclinical Research and Technology (CePT)
  2. European Regional Development Fund
  3. Innovative Economy Programme, The National Cohesion Strategy of Poland
  4. NIH [R00DK099254, T32DK007257-37, T32GM008203-29]
  5. Welch Foundation [I-1911]
  6. Cancer Prevention Research Institute of Texas (CPRIT) [RP170674]
  7. Polish National Science Centre [2014/15/B/NZ1/03359, 2017/25/B/NZ1/01883]

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The molecular chaperone HSP90 facilitates the folding of several client proteins, including innate immune receptors and protein kinases. HSP90 is an essential component of plant and animal immunity, yet pathogenic strategies that directly target the chaperone have not been described. Here, we identify the HopBF1 family of bacterial effectors as eukaryotic-specific HSP90 protein kinases. Hop BF1 adopts a minimal protein kinase fold that is recognized by HSP90 as a host client. As a result, HopBF1 phosphoryiates HSP90 to completely inhibit the chaperone's ATPase activity. We demonstrate that phosphorylation of HSP90 prevents activation of immune receptors that trigger the hypersensitive response in plants. Consequently, HopBF1 -dependent phosphorylation of HSP90 is sufficient to induce severe disease symptoms in plants infected with the bacterial pathogen, Pseudomonas syringae. Collectively, our results uncover a family of bacterial effector kinases with toxin-like properties and reveal a previously unrecognized betrayal mechanism by which bacterial pathogens modulate host immunity.

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