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A Bacterial Effecto...
A Bacterial Effector Mimics a Host HSP90 Client to Undermine Immunity
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- Lopez, Victor A. (author)
- University of Texas Southwestern Medical Center
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- Park, Brenden C. (author)
- University of Texas Southwestern Medical Center
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- Nowak, Dominika (author)
- Institute of Biochemistry and Biophysics of the Polish Academy of Sciences
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- Sreelatha, Anju (author)
- University of Texas Southwestern Medical Center
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- Zembek, Patrycja (author)
- Institute of Biochemistry and Biophysics of the Polish Academy of Sciences
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- Fernandez, Jessie (author)
- University of Texas Southwestern Medical Center
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- Servage, Kelly A. (author)
- University of Texas Southwestern Medical Center,Howard Hughes Medical Institute
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- Gradowski, Marcin (author)
- Warsaw University of Life Sciences
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- Hennig, Jacek (author)
- Institute of Biochemistry and Biophysics of the Polish Academy of Sciences
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- Tomchick, Diana R. (author)
- University of Texas Southwestern Medical Center
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- Pawłowski, Krzysztof (author)
- Lund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups,Warsaw University of Life Sciences
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- Krzymowska, Magdalena (author)
- Institute of Biochemistry and Biophysics of the Polish Academy of Sciences
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- Tagliabracci, Vincent S. (author)
- University of Texas Southwestern Medical Center
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(creator_code:org_t)
- Elsevier BV, 2019
- 2019
- English.
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In: Cell. - : Elsevier BV. - 0092-8674. ; 179:1, s. 21-218
- Related links:
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http://dx.doi.org/10...
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http://www.cell.com/...
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Abstract
Subject headings
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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. 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Cellbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Cell Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Immunologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Immunology (hsv//eng)
Keyword
- chaperone
- effector
- HopBF1
- HSP90
- immunity
- kinase
- phosphorylation
- Pseudomonas syringae
Publication and Content Type
- art (subject category)
- ref (subject category)
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Cell
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- By the author/editor
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Lopez, Victor A.
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Park, Brenden C.
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Nowak, Dominika
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Sreelatha, Anju
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Zembek, Patrycja
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Fernandez, Jessi ...
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show more...
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Servage, Kelly A ...
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Gradowski, Marci ...
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Hennig, Jacek
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Tomchick, Diana ...
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Pawłowski, Krzys ...
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Krzymowska, Magd ...
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Tagliabracci, Vi ...
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Cell Biology
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Immunology
- Articles in the publication
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Cell
- By the university
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Lund University