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HSP70 as a mediator of host-pathogen interaction in Arabidopsis thaliana during Plasmodiophora brassicae infection

ABSTRACT: The interaction between Plasmodiophora brassicae and Arabidopsis thaliana reveals a complex struggle for cellular control, with HSP70 proteins playing a pivotal role. We demonstrate 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. Analysis of mutant lines revealed that mutations in HSP70 trigger compensatory accumulation of other isoforms, underscoring the dynamic regulation of the chaperone network. Proteomic profiling of root galls during infection showed strong correlations between pathogen load and the abundance of Plasmodiophora HSP70 protein CEO96729. Interactomics analyses revealed that CEO96729 interacts with host proteins involved in Plasmodiophora responses, including extracellular GDSL esterase/lipase, and forms heterodimers with host HSP70 isoforms. These findings suggest that Plasmodiophora hijacks the host's chaperone machinery to facilitate its infection, offering a potential explanation for the observed modulation of disease progression in HSP70 mutants. Notably, the results also point to possible interactions with key enzymes in host physiology, including catalase 2, essential for ROS metabolism, and nitrilase, critical for auxin biosynthesis and root gall formation. These interactions highlight the potential involvement of CEO96729 in manipulating host cellular processes and raise the intriguing possibility of an unexpected role for this pathogen-derived HSP70 ortholog within the host cell. Collectively, our study highlights the multifaceted roles of HSP70 proteins in Plasmodiophora pathogenicity and host-pathogen interactions, offering insights into chaperone-mediated processes in plant immunity and infection dynamics.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Root

SUBMITTER: Martin Cerny

LAB HEAD: Martin Cerny

PROVIDER: PXD059131 | Pride | 2025-05-21

REPOSITORIES: Pride

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Project description:Protein aggregation is a hallmark of many neurodegenerative diseases. In order to cope with misfolding and aggregation, cells have evolved an elaborate network of molecular chaperones, composed of different families. But while chaperoning mechanisms for different families are well established, functional and regulatory diversification within chaperone families is still largely a mystery. Here we decided to explore chaperone functional diversity, through the lens of pathological aggregation. We revealed that different naturally-occurring isoforms of DNAJ chaperones showed differential effects on different types of aggregates. We performed a chaperone screen for modulators of two neurodegeneration-related aggregating proteins, the Huntington’s disease-related HTT-polyQ, and the ALS-related mutant FUS (mutFUS). The screen identified known modulators of HTT-polyQ aggregation, confirming the validity of our approach. Surprisingly, modulators of mutFUS aggregation were completely different than those of HTT-polyQ. Interestingly, different naturally-occurring isoforms of DNAJ chaperones had opposing effects on HTT-polyQ vs. mutFUS aggregation. We identified a complex of the full length (FL) DNAJB14 and DNAJB12 isoforms which substantially alleviated mutFUS aggregation, in an HSP70-dependent manner. Their naturally occurring short isoforms were unable to form the complex, nor to interact with HSP70, and lost their ability to reduce mutFUS aggregation. In contrast, the short isoform of DNAJB12 significantly alleviated HTT-polyQ aggregation, while DNAJB12-FL aggravated HTT-polyQ aggregation. Finally, we demonstrated that full-length DNAJB14 ameliorated mutFUS aggregation compared to DNAJB14-short in primary neurons. Together, our data unraveled distinct molecular properties required for aggregation protection in different neurodegenerative diseases, and revealed a new layer of complexity of the chaperone network elicited by naturally occurring J-protein isoforms, highlighting functional diversity among the DNAJ family.

			Action	DRS
	PB-Col-2.msf	Msf
	PB-Col-2.raw	Raw
	PB-Col-3.msf	Msf
	PB-Col-3.raw	Raw
	PB-Col-4.msf	Msf

Dataset Information

HSP70 as a mediator of host-pathogen interaction in Arabidopsis thaliana during Plasmodiophora brassicae infection

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