title: Activity profiling reveals changes in the diversity and activity of proteins in Arabidopsis roots in response to nematode infection.
abstract: Cyst nematodes are obligate, sedentary endoparasites with a highly specialised biology and a huge economic impact in agriculture. Successful parasitism involves morphological and physiological modifications of the host cells which lead to the formation of specialised syncytial feeding structures in roots. The development of the syncytium is aided by a cocktail of nematode effectors that manipulate the host plant activities in a complex network of interactions through post-translational modifications. Traditional transcriptomic and proteomic approaches cannot display this functional proteomic information. Activity-based protein profiling (ABPP) is a powerful technology that can be used to investigate the activity of the proteome through activity-based probes. To better understand the functional proteomics of syncytium, ABPP was conducted on syncytia induced by the beet cyst nematode Heterodera schachtii in Arabidopsis roots. Our results demonstrated that the activity of several enzymes is differentially regulated in the syncytium compared to the control roots. Among those specifically activated in the syncytium are a putative S-formyl-glutathione hydrolase (SFGH), a putative methylesterase (MES) and two unidentified enzymes. In contrast, the activities of vacuolar processing enzymes (VPEs) are specifically suppressed in the syncytium. Competition labelling, quantitative gene expression and T-DNA knock-out mutants were used to further characterise the roles of the differentially regulated enzymes during plant-nematode interaction. In conclusion, our study will open the door to generate a comprehensive and integrated view of the host-pathogen warfare that results in the formation of long-term feeding sites for pathogens.
authors.affiliation: Rheinische Friedrich-Wilhelms-University of Bonn, INRES - Molecular Phytomedicine, Karlrobert-Kreiten-Straße 13, 53115 Bonn, Germany. Electronic address: mhuetten@uni-bonn.de.
authors.forename: Marion
authors.initials: M
authors.lastname: Hütten
authors.affiliation: Rheinische Friedrich-Wilhelms-University of Bonn, INRES - Molecular Phytomedicine, Karlrobert-Kreiten-Straße 13, 53115 Bonn, Germany. Electronic address: mel-ge@freenet.de.
authors.forename: Melanie
authors.initials: M
authors.lastname: Geukes
authors.affiliation: Plant Chemetics Lab, Max-Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829 Cologne, Germany; Botanical Institute and Cluster of Excellence on Plant Sciences, University of Cologne, 50674 Cologne, Germany. Electronic address: misas@mpipz.mpg.de.
authors.forename: Johana C
authors.initials: JC
authors.lastname: Misas-Villamil
authors.affiliation: Plant Chemetics Lab, Max-Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829 Cologne, Germany; Plant Chemetics Lab, Department of Plant Sciences, University of Oxford, South Parks Road, OX1 3UB Oxford, UK. Electronic address: renier.vanderhoorn@plants.ox.ac.uk.
authors.forename: Renier A L
authors.initials: RA
authors.lastname: van der Hoorn
authors.affiliation: Rheinische Friedrich-Wilhelms-University of Bonn, INRES - Molecular Phytomedicine, Karlrobert-Kreiten-Straße 13, 53115 Bonn, Germany. Electronic address: grundler@uni-bonn.de.
authors.forename: Florian M W
authors.initials: FM
authors.lastname: Grundler
authors.affiliation: Rheinische Friedrich-Wilhelms-University of Bonn, INRES - Molecular Phytomedicine, Karlrobert-Kreiten-Straße 13, 53115 Bonn, Germany. Electronic address: siddique@uni-bonn.de.
authors.forename: Shahid
authors.initials: S
authors.lastname: Siddique
mesh_terms: D000818:Animals; D017360:Arabidopsis / Q000378:metabolism* / Q000469:parasitology; D029681:Arabidopsis Proteins / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D015726:Giant Cells / Q000378:metabolism / Q000469:parasitology; D006790:Host-Parasite Interactions; D018517:Plant Roots / Q000378:metabolism / Q000469:parasitology; D011499:Protein Processing, Post-Translational; D040901:Proteomics; D013869:Thiolester Hydrolases / Q000378:metabolism; D014431:Tylenchoidea / Q000502:physiology*
chemical_list: D029681:Arabidopsis Proteins; D013869:Thiolester Hydrolases; C020149:s-formylglutathione hydrolase
keywords: ABPP; Activity-based protein profiling; Arabidopsis thaliana; Heterodera schachtii; Plant–nematode interaction; Proteome; Syncytium