Evidence map›Paper›PMID 31522888›Full record

ArticleCell2019

A Bacterial Effector Mimics a Host HSP90 Client to Undermine Immunity.

Victor A Lopez, Brenden C Park, Dominika Nowak, Anju Sreelatha, Patrycja Zembek, Jessie Fernandez, Kelly A Servage, Marcin Gradowski, Jacek Hennig, Diana R Tomchick and 3 more

Open access · greenAbstract read
In one paragraph

Article in Cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.3field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
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  9. Experimental Approaches to Visualize Effector Protein Translocation During Host-Pathogen Interactions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  10. An Insect Effector Mimics Its Host Immune Regulator to Undermine Plant Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  11. Review
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  14. Biochemical and structural insights into a 5' to 3' RNA ligase reveal a potential role in tRNA ligation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 3 countries.

Victor A LopezDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Brenden C ParkDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Dominika NowakInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Anju SreelathaDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Patrycja ZembekInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Jessie FernandezDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Kelly A ServageDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Howard Hughes Medical Institute, Dallas, TX 75390, USA.
Marcin GradowskiWarsaw University of Life Sciences, Warsaw, Poland.
Jacek HennigInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Diana R TomchickDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Krzysztof PawłowskiWarsaw University of Life Sciences, Warsaw, Poland; Lund University, Lund, Sweden.
Magdalena KrzymowskaInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Vincent S TagliabracciDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Harold C. Simmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Hamon Center for Regenerative Science and Medicine, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address: vincent.tagliabracci@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · USInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PLWarsaw University of Life Sciences · PL

Funding

DIVISION OF CELL &MOLECULAR BIOLOGY TRAINING PROGRAMT32GM008203 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI COBB, MELANIE H. · 1987 to 2018
$7.0M
RENAL CONTROL OF BODY COMPOSITION AND BLOOD PRESSURET32DK007257 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI BAUM, MICHEL GERARD, MOE, ORSON W · 1986 to 2021
$5.0M
Phosphorylation of FGF23 coordinates crosstalk between the skeleton and kidneyR00DK099254 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI TAGLIABRACCI, VINCENT SCOTT · 2015 to 2017
$746k
Single Crystal X-ray Diffractometer equipped with Hybrid Pixel Array Detector and In Situ Crystallization Plate Screening CapS10OD025018 · OD · UT SOUTHWESTERN MEDICAL CENTER · PI TOMCHICK, DIANA R. · 2018 to 2018
$453k
NIDDK NIH HHS R00 DK099254NIDDK NIH HHS T32 DK007257NIGMS NIH HHS T32 GM008203NIH HHS S10 OD025018
6 · The paper itself

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 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.

Indexed as

Adenosine TriphosphatasesArabidopsisArabidopsis ProteinsBacterial ProteinsHEK293 CellsHeLa CellsHost Microbial InteractionsHSP90 Heat-Shock ProteinsHumansMolecular MimicryPhosphorylationPlant ImmunityPlasmidsProtein BindingProtein FoldingProtein KinasesAdenosine TriphosphatasesArabidopsis ProteinsBacterial ProteinsHSP90 Heat-Shock ProteinsProtein KinaseschaperoneeffectorHopBF1HSP90immunitykinasephosphorylationPseudomonas syringae

Identifiers

PMID31522888
PMCPMC6754304
OpenAlexW2972659958

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.