{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067464/SDRF_Metadates.tsv"],"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067464/All_data_after_MaxQuanttable.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067464/parameters.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067464/checksum.txt"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067464/uniprotkb_leishmania_infantum_AND_exist_2025_01_07.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067464/nickel_agarose_raw_data_triplicate.zip.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067464/anti-HA_raw_data_triplicate.zip.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067464/anti-myc_raw_data_triplicate.zip.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067464/Output_maxquant.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["frt@ufscar.br"],"submitter":["Wesley Regatieri"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry"],"disease":["Visceral Leishmaniasis"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067464"],"sample_protocol":["Promastigote forms of Leishmania infantum expressing Cas9/T7RNA polymerase were washed twice with PBS and lysed in cold NP-40 buffer (50 mM Tris-HCl, pH 7.2, 225 mM KCl, 1% NP-40) supplemented with protease inhibitors (SIGMAFAST, Sigma-Aldrich) and phosphatase inhibitors (10 mM NaF, 1 mM Na₃VO₄) using three freeze–thaw cycles (liquid nitrogen/room temperature). Lysates were incubated on ice for 30 min and centrifuged at 14,000 × g for 20 min at 4 °C. Protein concentration was determined by Bradford assay (Sigma-Aldrich). For each condition, 20 mg of protein was incubated for 3 h at 4 °C under rotation with 60 μL of the following beads: anti-myc (Sigma-Aldrich, #E6654), anti-HA (#E6779) or Ni-NTA (Cytiva 17-5318-01). Beads were washed with 5 × 500 μL cold lysis buffer and 3 × 500 μL cold wash buffer (10 mM HEPES, pH 7.9, 1.5 mM MgCl₂, 225 mM KCl). The proteins were eluted with 6M guanidine for 10 minutes at 22 °C prior to on-bead digestion. The eluted proteins were diluted to 1 M guanidine in 50 mM ammonium bicarbonate, and proteins were reduced with 10 mM dithiothreitol (DTT) for 20 min at 56 °C and alkylated with 20 mM iodoacetamide (IAA) in the dark for 15 min at room temperature. Two micrograms of trypsin gold, mass spectrometry grade (Promega #V5280), was added and digestion proceeded overnight at 37 °C. The reaction was stopped by adding trifluoroacetic acid (TFA) to a final concentration of 1%, followed by a 5 min incubation. Samples were reconstituted in 10 μL of formic acid, and 1 μL was injected for analysis on an ETD-enabled Orbitrap Velos mass spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) coupled to an EASY-nLC system (Proxeon Biosystems, West Palm Beach, FL, USA) via a Proxeon nanoelectrospray ion source."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Protein identification was performed in MaxQuant (versions 2.0.3 and 2.6.7.0) against the Leishmania infantum JPCM5 protein database obtained from UniProtKB (release 2025_01_07). Carbamidomethylation of cysteine residues was set as a fixed modification, while N-terminal acetylation and methionine oxidation were included as variable modifications. Enzyme specificity was defined as trypsin, allowing a maximum of one missed cleavage, and a minimum peptide length of 7 amino acids was required. Mass tolerance was set to 10 ppm for precursor ions and 1 Da for fragment ions. Protein identification was filtered at a maximum false discovery rate (FDR) of 1% at both peptide and protein levels, using a reverse target-decoy database strategy with reversed peptide sequences as decoy entries. All raw mass spectrometry files and associated search parameters are publicly available via the ProteomeXchange Consortium through the PRIDE repository under the dataset identifier PXD067464. The resulting ProteinGroups output tables were processed with the exclusion of reverse sequences and contaminant entries. Label-free quantification (LFQ) was performed using normalized LFQ intensity values, which were subsequently log2-transformed. Proteins identified only by site or by a single modified peptide were removed to ensure high-confidence identifications. Further filtering steps were applied to retain proteins with sufficient quantitative information. Only proteins presenting detectable LFQ signal and quantified in at least two out of three replicates within each experimental group were considered for downstream analyses. Additionally, at least one valid LFQ intensity value per group was required. For comparative analyses, proteins were considered as hits only when LFQ intensity values were detected in at least two out of three replicates within each experimental group (HA, His, and Myc). Filtered datasets were then organized into independent tables corresponding to each group, and proteins consistently identified across all groups were selected and further classified according to their annotated biological functions."],"omics_type":["Proteomics"],"labhead":["Felipe Roberti"],"instrument_platform":[""],"labhead_affiliation":["Department of Genetics and Evolution, Federal University of São Carlos, São Paulo, Brazil"],"submission_type":["PARTIAL"],"species":["Leishmania Infantum Jpcm5"],"submitter_mail":["wesley.klaysson@hotmail.com"],"publication":["10.1016/J.DIB.2026.112840"],"submitter_affiliation":["Federal University of São Carlos"],"submitter_country":["Brazil"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic Dataset of Non-Specific Interactors in Leishmania infantum","description":"This dataset provides a proteomic resource of non-specific protein interactions in Leishmania infantum identified by affinity purification coupled to mass spectrometry (AP-MS/MS). Protein extracts from promastigotes expressing Cas9/T7 RNA polymerase were subjected to immunoprecipitation using HA, myc, and His affinity systems, followed by LC–MS/MS analysis. Raw spectral data were processed using MaxQuant against the L. infantum reference proteome from UniProtKB. The dataset includes raw mass spectrometry files, peptide and protein identification tables, and label-free quantification (LFQ) data, all publicly available via the ProteomeXchange Consortium under the identifier PXD067464. After data filtering, a total of 566 unique proteins were identified across all conditions, including 60 proteins consistently detected in all three affinity systems, representing putative non-specific binders. Among these, metabolism-related proteins (30%) and ribosomal components (28%) were the most abundant functional classes. This dataset provides a valuable reference for background protein binding in AP-MS/MS experiments in Leishmania , supporting improved interpretation of interactome studies and benchmarking of affinity purification strategies. 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