{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD074932/checksum.txt"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD074932/MEP32b.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD074932/MEP32a.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD074932/MEP32.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD074932/Contaminantes.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["mepeichoto@yahoo.com.ar"],"submitter":["Maria Pia Valacco"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Hemolysis","Megalopygidae","Losac","Proteolytic enzymes","Procoagulant activity","Toxins"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074932"],"sample_protocol":["Proteomic analyses were performed at the Proteomics Core Facility CEQUIBIEM (University of Buenos Aires/CONICET) using a protein fraction of 33 kDa obtained by RP-HPLC and excised from an SDS-PAGE gel band stained with Coomassie G-250. Briefly, 50 µg of protein was treated with 8 M urea for 15 min at 80 °C, 100 mM dithiothreitol (DTT) for 30 min at 60 °C, and then 150 mM iodoacetamide (IAA) for 30 min at room temperature to disrupt tertiary structures and reduce/alkylate disulfide bonds. Samples were diluted in 50 mM Tris-HCl buffer (pH 7.5) and digested with sequencing-grade trypsin (20 ng/µL; Promega V5111) in 50 mM ammonium bicarbonate. Digestion was carried out overnight at 37 °C and stopped with 5% formic acid (FA). Peptides were desalted prior to LC-MS/MS analysis using C18 zip tips (Merck Millipore), according to the manufacturer’s instructions. The digests were analyzed by nanoLC-MS/MS using a Thermo Scientific Q Exactive mass spectrometer coupled to an EASY-nLC 1000 nanoHPLC system (Thermo Scientific). Approximately 1 µg of peptides was loaded onto a reverse-phase column (C18, 2 µm, 100 Å, 50 µm × 150 mm; Easy-Spray Column PepMap RSLC, P/N ES801) and eluted over 120 min. The flow rate was 300 nL/min with a gradient from 7% solvent B (5 min) to 35% (120 min). Solvent A was 0.1% FA in water, and solvent B was 0.1% FA in acetonitrile. Injection volume was 2 µL. The MS system included a high-energy collision dissociation (HCD) cell for fragmentation and an Orbitrap analyzer. Electrospray ionization was performed at 3.5 kV using an EASY-Spray source. XCalibur 3.0.63 (Thermo Scientific) was used for data acquisition and instrument control, enabling peptide identification during chromatographic separation. Full-scan MS spectra were acquired in the Orbitrap analyzer over a mass range of 400–1800 m/z at a resolution of 70,000 at 400 m/z. The 12 most intense ions per cycle were sequentially isolated, fragmented by HCD, and measured in the Orbitrap. Peptides with a charge of +1 or unassigned charge state were excluded from MS2 fragmentation."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw data were processed using Proteome Discoverer software (version 2.2; Thermo Scientific) and searched against a Lepidoptera protein sequence database with trypsin specificity and a maximum of one missed cleavage per peptide. Searches were performed with a precursor mass tolerance of 10 ppm and product ion tolerance of 0.05 Da. Static modifications included carbamidomethylation of cysteine, and dynamic modifications included methionine oxidation and N-terminal acetylation. Protein hits were filtered for high-confidence peptide matches with a maximum protein and peptide false discovery rate of 1%, calculated using a reverse database strategy. Additional searches were conducted against databases containing venom-related sequences from various caterpillar species, including Megalopygidae, Lonomia obliqua prothrombin activator protein, and proteins reported in UniProt for Podalia orsilochus and L. obliqua.    Raw mass spectrometry data files were processed using standard proteomics workflows. Database searches were performed using appropriate search engines against a protein database relevant to the studied organism, including common contaminant proteins. Trypsin was specified as the proteolytic enzyme, allowing for a limited number of missed cleavages. Mass tolerances were set according to instrument specifications. Variable modifications included common post-translational modifications, and false discovery rate (FDR) was controlled at 1% at the peptide and protein levels. The resulting identifications were used for downstream qualitative analysis."],"omics_type":["Proteomics"],"labhead":["Maria Elisa Paichoto"],"instrument_platform":[""],"labhead_affiliation":["INSTITUTO DE BIOLOGIA SUBTROPICAL - NODO PUERTO IGUAZU - CENTRO CIENTIFICO TECNOLOGICO CONICET - NORDESTE - CONSEJO NACIONAL DE INVESTIGACIONES CIENTIFICAS Y TECNICAS -"],"submission_type":["PARTIAL"],"species":["Megalopygidae Sp. Bold:aaa3544"],"publication":["41881159 Gritti MA, Martínez ME, Gonzalez KY, Lobo López K, Teibler GP, Santoro ML, Peichoto ME. Beyond envenomation: functional dissection of Podalia orsilochus venom uncovers a procoagulant protein and additional toxic activities. Toxicon. 2026 276:109086 10.1016/j.toxicon.2026.109086"],"submitter_mail":["pvalacco@qb.fcen.uba.ar"],"submitter_affiliation":["University of Buenos Aires"],"submitter_country":["Argentina"],"additional_accession":[]},"is_claimable":false,"name":"Beyond envenomation: functional dissection of Podalia orsilochus venom uncovers a procoagulant protein and additional toxic activities","description":"Envenomation by urticating caterpillars of the family Megalopygidae is an underestimated public health issue in South America, with Podalia orsilochus being the main species implicated in cases reported in northeastern Argentina. This study aimed to characterize the toxicological properties of its venom, focusing on hematological and hemostatic effects. Venom extracts were analyzed using electrophoresis, zymography, hemolysis and coagulation assays, and chromatographic fractionation followed by immunodetection. Electrophoretic profiles revealed predominant proteins in the 10–37 kDa range, with several gelatinolytic bands detected by zymography. The venom exhibited thrombin-like and dose-dependent procoagulant activity, although weaker than that of Lonomia obliqua. A mild, direct hemolytic effect on human erythrocytes was observed, associated with degradation of Band 3, a major membrane protein. A 33-kDa protein was purified and shown to induce procoagulant activity while cross-reacting with antibodies against Losac, a Factor X-activating protein from L. obliqua venom, indicating the presence of Losac-like toxins in P. orsilochus. In conclusion, P. orsilochus venom contains components with proteolytic, hemolytic, and coagulotoxic activities, including a Losac-like protein, expanding current knowledge of lepidopteran venoms and their potential impact on human 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