HSP70 as a Mediator of Host–Pathogen Interaction in Arabidopsis thaliana During Plasmodiophora brassicae Infection
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F25%3A43927106" target="_blank" >RIV/62156489:43210/25:43927106 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1111/ppl.70309" target="_blank" >https://doi.org/10.1111/ppl.70309</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/ppl.70309" target="_blank" >10.1111/ppl.70309</a>
Alternative languages
Result language
angličtina
Original language name
HSP70 as a Mediator of Host–Pathogen Interaction in Arabidopsis thaliana During Plasmodiophora brassicae Infection
Original language description
Plasmodiophora brassicae is one of the most devastating threats to Brassicaceae crops. However, the molecular mechanisms underlying clubroot disease remain unclear. Initial proteomics results led us to hypothesize that HSP70 proteins regulate host-P. brassicae interactions by modulating both plant defenses and pathogen activity. Using the Arabidopsis thaliana-P. brassicae model system, we studied the role of HSP70 proteins in detail. Through a combination of proteomics and mutant phenotype analyses, we indicate that Plasmodiophora infection induces HSP70 accumulation in Arabidopsis roots, and mutations in specific HSP70 isoforms either promote (HSP70-1, HSP70-13, HSP70-14) or suppress (HSP70-5, HSP70-12) the onset of clubroot disease. Proteomic profiling of root galls showed strong correlations between infection severity and pathogen-derived HSP70 protein CEO96729. Interactomics analyses revealed that CEO96729 interacts with host proteins involved in plant response to Plasmodiophora infection, including an extracellular GDSL esterase/lipase with a putative role in long-distance signaling, and that CEO96729 forms heterodimers with host HSP70 isoforms. These findings suggest that Plasmodiophora hijacks the host chaperone machinery to facilitate infection, offering a potential explanation for the observed modulation of disease progression in HSP70 mutants. Notably, the results also point to possible intracellular interactions with key enzymes in host physiology, including catalase 2, essential for ROS metabolism, and nitrilase, critical for auxin biosynthesis and root gall formation. Collectively, our study highlights the multifaceted roles of HSP70 proteins in Plasmodiophora pathogenicity and host-pathogen interactions, providing insights into chaperone-mediated processes in plant immunity and infection dynamics.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
40106 - Agronomy, plant breeding and plant protection; (Agricultural biotechnology to be 4.4)
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Physiologia Plantarum
ISSN
0031-9317
e-ISSN
1399-3054
Volume of the periodical
177
Issue of the periodical within the volume
3
Country of publishing house
US - UNITED STATES
Number of pages
16
Pages from-to
"e70309"
UT code for WoS article
001501273400001
EID of the result in the Scopus database
2-s2.0-105007634207