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Aasegg Araya"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Australian funnel-web spider","Inhibitor cystine knot","Hi1a","Mygalomorphae","Spider venom","Pi-hexatoxin","Bivalent peptides"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070138"],"tissue":["Venom"],"sample_protocol":["The female individual of H.cerberea was collected in 2020 from the Central Coast, NSW, Australia with the assistance of the Australian Reptile Park (Gosford, NSW, Australia) and housed individually at 23-25 °C in a plastic container. Forceps were used to aggravate the spider until venom was secreted and collected continuously by aspiration until we could obtain no more venom. The venom was lyophilized and stored on -30 °C prior to shipment.   In addition, a total of 11 spider species of Mygalomorphae (see full species list in SI Table S6) were purchased from Exo-Pet (https://www.exo-pet.de) and Zoohaus W&S (https://www.zoohaus-ws.de) and housed individually at 23 °C in plastic containers. Of these, 10 were milked exhaustively for venom (only adult or subadult specimens) through biting over a plastic film and electrically stimulating the venom glands for secretion until we could not obtain more venom. The venom samples were immediately dissolved in 5-10 µL MilliQ water (depending on the amount of obtained venom) and snap frozen on liquid nitrogen.  The total of 11 venom samples (3-5 µL) were either dissolved in 80 mM ammonium bicarbonate (samples that were stored in MilliQ water) or resuspended in 10% acetonitrile (ACN) in 100 mM ammonium bicarbonate (lyophilized venom) and subsequently reduced with DTT and alkylated with iodoacetamide (IAA). The reduced and alkylated samples were digested by incubating with a concentration of ~20 ng/mL trypsin overnight at 37°C. The digested samples were washed and resuspended in a final concentration of 5% ACN and 1% formic acid (FA), prior to peptide identification by LC-MS/MS on a UHPLC-TimsTOF Pro mass spectrometer (Bruker)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The MS/MS spectra were searched against the transcriptomic sequence databases custom to each sample using MaxQuant in DDA mode, using a default decoy-based false discovery rate of 0.01% and only including the most common post-translational modifications in the search. Carbamidomethyl (C) was set as a fixed modification. For in-solution digests, Trypsin/P specificity was applied, allowing up to two missed cleavages, but no fixed modifications were set. For both sample types, variable modifications included Oxidation (M), Glu->pyro-Glu, Amidated (Protein C-term), and Acetyl (Protein N-term). Output was evaluated and processed with an in-house filtering script that uses SignalP v.5.0 to predict signal peptides and sort the database sequences that have peptide hits. Finally, we added a search with MSFragger  for comparison with default settings."],"omics_type":["Proteomics"],"labhead":["Eivind Andreas Baste Undheim"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["University of Oslo, Department of Biosciences, Centre for Ecological and Evolutionary Synthesis"],"species":["Chaetopelma Olivaceum","Chilobrachys","Fufius","Lasiodora Parahybana","Harpactira","Cyrtocarenum Grajum","Brachypelma Boehmei","Hadronyche Cerberea","Avicularia Avicularia"],"publication":["41877653 Araya RA, Maurstad MF, Wilson DT, Rash LD, Mobli M, Jakobsen KS, Undheim EAB. Ancient origin and dynamic evolution of bivalent spider toxins. Mol Biol Evol. 2026 43(5):msag076 10.1093/molbev/msag076"],"submitter_mail":["r.a.araya@ibv.uio.no"],"submitter_affiliation":["University of Oslo"],"submitter_country":["Norway"],"pubmed_abstract":["Bivalent peptide toxins comprising 2 cysteine-rich domains have evolved from single-domain precursors on multiple occasions in animal venoms, resulting in enhanced molecular target selectivity and avidity. Although bivalent toxins are emerging as prevalent in animal venoms, the genomic and evolutionary processes driving the transitions between single- and multi-domain architectures remain poorly understood. Here, we investigated the evolution of bivalent inhibitor cystine knot (ICK) toxins in spider venom. We first generated a genome assembly of the tree-dwelling funnel-web spider Hadronyche cerberea, revealing a massive expansion of ICK toxin-encoding genes, including the bivalent π-hexatoxin-Hc1a. All ICK toxin genes share a conserved 3-exon structure, flanked by transposable elements (TEs) that may have facilitated gene expansion. This gene structure is shared by the Hc1a subfamily, where the entire mature bivalent toxin is encoded by the third exon. Leveraging de novo transcriptome assemblies from 86 spider species along with venom proteomic data, we show that bivalency in the Hc1a subfamily is of ancient origin and evolved via intra-exonic duplication not involving introns. This was followed by domain expansion and recurrent domain losses mediated by point mutations, deletions, and unequal crossing-over facilitated by high interdomain sequence similarity. In contrast, the bivalent toxin DkTx from Cyriopagopus schmidti is confined to a small group of tarantulas, where it appears to have evolved once, with subsequent domain losses potentially linked to TE activity. Our findings reveal that singular events of domain duplication can give rise to complex, asymmetrical evolutionary trajectories shaped by gene instability and selective retention of functional domains."],"pubmed_title":["Ancient origin and dynamic evolution of bivalent spider toxins."],"pubmed_authors":["Araya Robin A RA, Maurstad Marius F MF, Wilson David T DT, Rash Lachlan D LD, Mobli Mehdi M, Jakobsen Kjetill S KS, Undheim Eivind A B EAB"],"additional_accession":[]},"is_claimable":false,"name":"Ancient origin and dynamic evolution of bivalent spider toxins","description":"Bivalent peptide toxins comprising two cysteine-rich domains have evolved from single-domain precursors on multiple occasions in animal venoms, resulting in enhanced molecular target selectivity and avidity. Although bivalent toxins are emerging as prevalent in animal venoms, the genomic and evolutionary processes driving the transitions between single- and multi-domain architectures remain poorly understood. Here, we investigated the evolution of bivalent inhibitor cystine knot (ICK) toxins in spider venom. We first generated generate a genome assembly of the tree-dwelling funnel-web spider Hadronyche cerberea, revealing a massive expansion of ICK toxin-encoding genes, including the bivalent π-hexatoxin-Hc1a. All ICK toxin genes share a conserved three-exon-structure, flanked by transposable elements (TEs) that may have facilitated gene expansion. This gene structure is shared by the Hc1a family, where the entire mature bivalent toxin is encoded by the third exon. Leveraging de novo transcriptome assemblies of 86 spider species along with venom proteomic data, we show that bivalency in the Hc1a family is of ancient origin, but with recurrent domain expansions and losses due to point mutations, deletions, and unequal crossing-over facilitated by high interdomain sequence similarity. In contrast, the bivalent toxin DkTx from Cyriopagopus schmidti appears to have evolved once in a restricted group of tarantulas. While we also find here multiple domain loss events, these are potentially facilitated by TEs as opposed to pseudogenisation or unequal crossing over. Our findings reveal that singular events of domain duplication can give rise to complex, asymmetrical evolutionary trajectories shaped by gene instability and selective retention of functional domains.","dates":{"publication":"2026-06-08","submission":"2025-10-31"},"accession":"PXD070138","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:1538","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211"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