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Wang"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"disease":["Parasitic Helminthiasis Infectious Disease"],"software":[""],"submitter_keywords":["Pisa assay","Haemonchus contortus","Anthelmintic","Proteomics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075263"],"tissue":["Stem Cell","Whole Body"],"sample_protocol":["Each sample was denatured with equal volume of 16 M urea in 200 mM TEAB solution for 30 min at 37 °C and conducted in-solution digestion using established protocol (Wang et al., 2025). Briefly, individual samples from each treatment were reduced with 10 mM tris (2-carboxyethyl) phosphine (TCEP) at 55 °C for 45 min, then alkylated with 55 mM iodoacetamide in the dark at 22 °C for 30 min, followed by a trypsin (Pierce, USA) digestion at 37 °C for 16 h. The tryptic samples were acidified with 1.0% (v/v) formic acid, purified using Oasis HLB cartridges (Waters, USA). All digested peptide samples were freeze-dried.  Subsequently, peptide samples were labelled with tandem mass tags (TMTs) using an established protocol (Zecha et al., 2019). In brief, freeze-dried peptide samples were resuspended in 60 µL of 50 mM Triethylammonium bicarbonate (TEAB) (pH 8.5) and mixed with a TMT10plex reagent (Thermo Fisher, US) that dissolved in 41 μl anhydrous acetonitrile. The 10th TMT channel corresponding to TMT10-131 was used as reference channel for labelling all studied samples. The TMT-peptide mixture was incubated for 1 h at 25 °C, with gentle shaking. Sequentially, a volume of 3.2 μl of 5% (w/v) hydroxylamine was added to the mixture and incubated for 15 min at 25 °C, with gentle shaking, to quench the reaction. Labelled peptides were combined accordingly and then desalted on Oasis HLB cartridges. Each mixed peptide sample was separated into eight fractions using the high pH reversed-phase peptide fractionation kit (Pierce, USA), according to the manufacturer's protocol. All fractions were freeze-dried prior to resuspension in aqueous 2% (w/v) acetonitrile and 0.05% (w/v) trifluoroacetic acid (TFA) before LC-MS/MS analysis."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Mass spectrometry data were processed using MaxQuant for the identification and quantification of peptides/proteins. Proteins were matched to those inferred from the full-length chromosome-contiguous genome of the Haecon-5 strain of H. contortus (Zheng et al., 2024). The TMT reagent was corrected for natural carbon isotopes and incomplete stable isotope incorporation. Fixed modifications of carbamidomethylation of cysteine. Trypsin/P was set as the protease with a maximum of 2 missed cleavages. Variable modifications are oxidation of methionine and acetylation of protein N-terminus. Protein and PSM false discovery rates (FDR) were both set at < 0.01. Reporter intensities from all PISA samples were normalised to the TMT10-131 channel corresponding to all samples to convert the intensity values to ratios. The normalised TMT reporter intensities ratios were retrieved from the “proteingroups.txt” file generated from MaxQuant analysis."],"omics_type":["Proteomics"],"labhead":["Robin Beat Gasser"],"instrument_platform":[""],"labhead_affiliation":["Department of Veterinary Biosciences, Melbourne Veterinary School, The University of Melbourne, Parkville, Victoria, 3052, Australia"],"submission_type":["PARTIAL"],"species":["Haemonchus Contortus (barber Pole Worm)"],"publication":["Not available"],"submitter_mail":["tao.wang1@unimelb.edu.au"],"submitter_affiliation":["The University of Melbourne"],"submitter_country":["Australia"],"additional_accession":[]},"is_claimable":false,"name":"Proteome integral solubility alteration (PISA) analysis of compound treated Haemonchus contortus","description":"This study applied the proteome integral solubility alteration (PISA) assay to infer molecular targets and protein–ligand interactions of candidate nematocidal compound in Haemonchus contortus. By monitoring compound-induced shifts in protein solubility across a temperature gradient, the analysis provided proteome-wide evidence of direct or indirect binding events in both adult female worms and in vitro-exsheathed third-stage larvae (xL3s). Protein extracts were prepared under standardised conditions, incubated with each test compound at ten times the LC₅₀, subjected to temperature challenges and then processed for tandem mass tag (TMT)-based quantitative proteomics using high-resolution LC-MS/MS. Resultant data sets were analysed via MaxQuant and Perseus, with protein identifications referenced to the annotated chromosome-scale genome of H. contortus 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