{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_FASP_GE8_01_56402_5600_ProteinSummary.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_lowmass_nodig_GE6_01_56412_5600_ProteinSummary.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_lowmass_dT_GE7_01_56407_5600_ProteinSummary.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_lowmass_nodig_GE6_01_56412_5600_PeptideSummary.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_lowmass_dT_GE7_01_56407_5600_PeptideSummary.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_FASP_GE8_01_56402_5600_PeptideSummary.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_lowmass_dT_GE7_01_56407.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_FASP_GE8_01_56402.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_lowmass_nodig_GE6_01_56412.xml"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_lowmass_dT_GE7_01_56407.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_lowmass_nodig_GE6_01_56412.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_FASP_GE8_01_56402.mgf"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_lowmass_nodig_GE6_01_56412_5600.group","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_lowmass_dT_GE7_01_56407_5600.group","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074241/4137_QTOF1_65IS_FASP_GE8_01_56402_5600.group"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["pekar@sci.muni.cz"],"submitter":["Ondrej Michalek"],"technology_type":["Mass Spectrometry","Top-down proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074241"],"tissue":["Venom Gland"],"sample_protocol":["Ammoxenus amphalodes spiders were collected in the open field in Langenhoven Park, Bloemfontein, South Africa (29°06.680'S, 26°09.540'E), in October 2019. Altogether, three males, 14 females and seven juveniles were collected. Spiders were kept singly in glass tubes (height: 6 cm, diameter: 1.5 cm) with moisturised gypsum on the bottom and stored at room temperature (22 °C) with a light-to-dark cycle of 16:8. Venom was obtained from Ammoxenus amphalodes spiders using an electrical milking technique (Eggs et al., 2015; Friedel & Nentwig, 1989; Kuhn-Nentwig et al., 1994). Briefly, a spider was anesthetised with CO2 for 2 min, placed on a stub, covered with a mesh, stimulated with an electric impulse, and the venom collected into a 0.5 µL glass microcapillary (#1-000-0005, Drummond, Birmingham, AL, USA) that was slid onto one of the fangs of the spider's chelicerae. Approximately 0.58 μL of pooled A. amphalodes venom was obtained by milking the spiders. The milked crude venom was diluted in 1 µL of ammonium acetate buffer (0.1 M, pH 6.1) and the diluted venom was stored at –80°C before further processing. We followed the same proteomics protocol as described in our previous study (Michálek et al., 2022). A venom sample was loaded onto a Vivacon 500 centrifugal filtration device with a 10 kDa molecular weight cut-off (Sartorius Stedim Biotech). The filter was washed with 50 μL of 50 mM NaHCO3, and the flow-through (peptidome fraction) was collected. The peptidome fraction was then split into two equal portions. One half was subjected to reduction and alkylation using the same reagents and amounts as for the protein concentrate (see below); the second half was analysed untreated. The protein concentrate retained in the Vivacon 500 device was mixed with 100 μL of 50 mM dithiothreitol and then incubated for 30 min at 57°C. After centrifugation, 100 μL of 50 mM iodoacetamide was added, and the filter was incubated in the dark for 30 min at 25°C. Following another centrifugation step, the filter was washed with 200 μL of 50 mM NaHCO3. Trypsin (sequencing grade, Promega) was then added to the filter, and digestion proceeded for 14 h at 37°C. Tryptic peptides were eluted by centrifugation, followed by two additional elutions with 50 μL of 50 mM NaHCO3. The peptides were extracted using a 1:1 mixture of 25% formic acid (FA) and acetonitrile (ACN) containing 0.001% poly(ethylene glycol) and then vacuum concentrated.  The peptide mixtures were analysed via liquid chromatography-tandem mass spectrometry (LC-MS/MS) using an Ultimate 3000 RSLCnano system (Thermo Fisher Scientific, Waltham, MA, USA) coupled to an Impact II Qq-Time-of-Flight mass spectrometer (Bruker, Bremen, Germany). Prior to LC separation, peptides were concentrated on a trap column (100 μm × 30 mm) filled with 3.5-μm X-Bridge BEH 130 C18 sorbent (Waters, Milford, MA, USA). Peptides were separated on an Acclaim Pepmap100 C18 column (3 µm particle size, 75 μm × 500 mm; Thermo Fisher Scientific) using the following solvent gradient (mobile phase A: 0.1% FA in water; mobile phase B: 0.1% FA in 80% ACN; 300 nL/min flow rate): elution started with 1% mobile phase B, gradually increasing to 56% over 50 min, then increasing linearly to 80% mobile phase B over the next 5 min, followed by isocratic elution with 80% mobile phase B for 10 min. The trapping column and analytical column were equilibrated prior to sample injection. The outlet of the analytical column was connected directly to the CaptiveSpray nanoBooster ion source (Bruker, Bremen, Germany). MS and MS/MS spectra were acquired using a data-dependent strategy with a 3-s cycle time. The mass range was set to m/z 150–2200, with precursor ions selected from the range m/z 300–2000. MS and MS/MS acquisition speeds were 2 Hz and 4–16 Hz, respectively, with MS/MS acquisition rate varying based on precursor intensity. MS data preprocessing, including recalibration, compound detection and charge deconvolution, was performed using DataAnalysis software (version 4.2 SR1; Bruker)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The proteomic and transcriptomic data were integrated to identify peptides and proteins present in the venom (Walker et al., 2020). The workflow was similar to that used in our previous study (Michálek et al., 2022). Mass spectral data were used to search a database of possible amino acid sequences derived from the venom-gland transcriptome using the Paragon and ProtGroup algorithms in ProteinPilot software (SCIEX, Framingham, MA, USA), applying a 95% confidence cut-off at the protein level. cDNA sequences encoding the identified toxins were re-mapped using Geneious software (version 2019.0.4, Biomatters, Auckland, New Zealand) to correct sequencing errors and to identify variants and missing termini. Precursor sequences were annotated using SignalP (Teufel et al., 2022), BLAST searches against the UniProtKB/Swiss-Prot database (Altschul et al., 1997; The UniProt Consortium, 2021), and HMMER searches against the Pfam database (Eddy, 2008; Finn et al., 2014).  Due to the larger size of many toxins (>5 kDa), the mature forms of very few toxins could be resolved from the native and reduced/alkylated datasets. Therefore, we predicted the mature forms by manually inspecting the sequences for prepropeptide sequences. Expression levels were calculated using Geneious software. Toxins were classified into families based on sequence similarity and their cysteine scaffolds, and they were named according to established nomenclature guidelines (King et al., 2008). Given the complexity of previous spider toxin classification systems, we chose not to extend these systems. The 'families' defined here are based solely on sequence similarity among the venom components within the Ammoxenus proteome. The structure of the five selected toxins was predicted using Alphafold3 (Abramson et al., 2024) and compared with the Protein Data Bank (PDB) structures using the Dali server (Holm et al., 2023)."],"omics_type":["Proteomics"],"labhead":["Stano Pekar"],"instrument_platform":[""],"labhead_affiliation":["Department of Botany and Zoology Faculty of Science, Masaryk University Kotlarska 2, 611 37 Brno, Czech Republic"],"submission_type":["PARTIAL"],"species":["Ammoxenus Amphalodes"],"submitter_mail":["michalek.ondrej@mail.muni.cz"],"publication":["10.1016/J.IBMB.2026.104563"],"submitter_affiliation":["Department of Botany and Zoology, Faculty of Science, Masaryk University"],"submitter_country":["Czechia"],"additional_accession":[]},"is_claimable":false,"name":"Venom proteome of the termite-eating spider Ammoxenus amphalodes","description":"Venoms are complex chemical arsenals that have evolved across various animal lineages for predation, defence, and other ecological functions. In predatory species, venom composition is often shaped by diet, potentially leading to unique toxin profiles. Spiders are the most diverse group of terrestrial venomous predators, yet the venoms of most species, including highly specialized stenophagous species with narrow trophic niches, remain poorly understood. In this study, we investigated the venom of Ammoxenus amphalodes, a spider that preys exclusively on termites, to explore its molecular composition and functional adaptations. Using a proteotranscriptomic approach, we identified 116 putative toxin sequences. Half of these were cysteine-rich peptides with distinct structural motifs, most of which diverge from known spider toxins containing an inhibitor-cystine-knot (ICK) motif. The venom proteome is dominated by two ammoxotoxin families, which together account for more than half of all transcripts, supporting the hypothesis that spiders with specialized diets have lower toxin diversity. We also identified a low proportion of larger venom proteins, including cholinesterases, phospholipases, immune proteins, carbonic anhydrases, and EF-hand proteins, which may serve housekeeping functions or play auxiliary roles in prey incapacitation. Bioassays with selected lab-produced peptides revealed one prey-specific peptide, U-AXTX(9)-Aa15, a member of the waprin family, which paralyses termites but not flies. The other peptides tested showed limited prey specificity, challenging assumptions of venom specialization. These findings provide new insights into the evolution of venom in dietary specialists and broaden the search for novel bioactive compounds with potential biotechnological 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