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A Bacterial Effector Mimics a Host HSP90 Client to Undermine Immunity

Lopez, Victor A. ; Park, Brenden C. ; Nowak, Dominika ; Sreelatha, Anju ; Zembek, Patrycja ; Fernandez, Jessie ; Servage, Kelly A. ; Gradowski, Marcin ; Hennig, Jacek and Tomchick, Diana R. , et al. (2019) In Cell 179(1). p.21-218
Abstract

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. HopBF1 adopts a minimal protein kinase fold that is recognized by HSP90 as a host client. As a result, HopBF1 phosphorylates 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... (More)

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. HopBF1 adopts a minimal protein kinase fold that is recognized by HSP90 as a host client. As a result, HopBF1 phosphorylates 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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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
chaperone, effector, HopBF1, HSP90, immunity, kinase, phosphorylation, Pseudomonas syringae
in
Cell
volume
179
issue
1
pages
21 - 218
publisher
Cell Press
external identifiers
  • scopus:85072226110
  • pmid:31522888
ISSN
0092-8674
DOI
10.1016/j.cell.2019.08.020
language
English
LU publication?
yes
id
18b16d3d-7bc6-42dc-a7d4-3cd4f1fd41d2
date added to LUP
2019-09-30 14:17:50
date last changed
2024-06-27 06:29:53
@article{18b16d3d-7bc6-42dc-a7d4-3cd4f1fd41d2,
  abstract     = {{<p>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. HopBF1 adopts a minimal protein kinase fold that is recognized by HSP90 as a host client. As a result, HopBF1 phosphorylates 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.</p>}},
  author       = {{Lopez, Victor A. and Park, Brenden C. and Nowak, Dominika and Sreelatha, Anju and Zembek, Patrycja and Fernandez, Jessie and Servage, Kelly A. and Gradowski, Marcin and Hennig, Jacek and Tomchick, Diana R. and Pawłowski, Krzysztof and Krzymowska, Magdalena and Tagliabracci, Vincent S.}},
  issn         = {{0092-8674}},
  keywords     = {{chaperone; effector; HopBF1; HSP90; immunity; kinase; phosphorylation; Pseudomonas syringae}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{21--218}},
  publisher    = {{Cell Press}},
  series       = {{Cell}},
  title        = {{A Bacterial Effector Mimics a Host HSP90 Client to Undermine Immunity}},
  url          = {{http://dx.doi.org/10.1016/j.cell.2019.08.020}},
  doi          = {{10.1016/j.cell.2019.08.020}},
  volume       = {{179}},
  year         = {{2019}},
}