{"refrec":{"BRefID":301544,"RR":"<b>Sousa, S.R.; McArthur, J.R.; Brust, A.; Bhola, R.F.; Rosengren, K.J.; Ragnarsson, L.; Dutertre, S.; Alewood, P.F.; Christie, M.J.; Adams, D.J.; Vetter, I.; Lewis, R.J.</b> (2018). Novel analgesic ω-conotoxins from the vermivorous cone snail <i>Conus moncuri</i> provide new insights into the evolution of conopeptides. <i>NPG Scientific Reports 8(1)</i>: 15 pp. <a href=\"https://dx.doi.org/10.1038/s41598-018-31245-4\" target=\"_blank\">https://dx.doi.org/10.1038/s41598-018-31245-4</a>","BEntID":293785,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>NPG Scientific Reports 8(1)</i>: 15 pp. <a href=\"https://dx.doi.org/10.1038/s41598-018-31245-4\" target=\"_blank\">https://dx.doi.org/10.1038/s41598-018-31245-4</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Sousa, S.R.; McArthur, J.R.; Brust, A.; Bhola, R.F.; Rosengren, K.J.; Ragnarsson, L.; Dutertre, S.; Alewood, P.F.; Christie, M.J.; Adams, D.J.; Vetter, I.; Lewis, R.J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Sousa, S.R. <i>et al.</i>","Englishabstract":"Cone snails are a diverse group of predatory marine invertebrates that deploy remarkably complex venoms to rapidly paralyse worm, mollusc or fish prey. ω-Conotoxins are neurotoxic peptides from cone snail venoms that inhibit Ca<sub>v</sub>2.2 voltage-gated calcium channel, demonstrating potential for pain management via intrathecal (IT) administration. Here, we isolated and characterized two novel ω-conotoxins, MoVIA and MoVIB from <i>Conus moncuri</i>, the first to be identified in vermivorous (worm-hunting) cone snails. MoVIA and MoVIB potently inhibited human Ca<sub>v</sub>2.2 in fluorimetric assays and rat Ca<sub>v</sub>2.2 in patch clamp studies, and both potently displaced radiolabeled ω-conotoxin GVIA (<sup>125</sup>I-GVIA) from human SH-SY5Y cells and fish brain membranes (IC<sub>50</sub> 2–9 pM). Intriguingly, an arginine at position 13 in MoVIA and MoVIB replaced the functionally critical tyrosine found in piscivorous ω-conotoxins. To investigate its role, we synthesized MoVIB-[R13Y] and MVIIA-[Y13R]. Interestingly, MVIIA-[Y13R] completely lost Ca<sub>v</sub>2.2 activity and MoVIB-[R13Y] had reduced activity, indicating that Arg at position 13 was preferred in these vermivorous ω-conotoxins whereas tyrosine 13 is preferred in piscivorous ω-conotoxins. MoVIB reversed pain behavior in a rat neuropathic pain model, confirming that vermivorous cone snails are a new source of analgesic ω-conotoxins. Given vermivorous cone snails are ancestral to piscivorous species, our findings support the repurposing of defensive venom peptides in the evolution of piscivorous Conidae.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Novel analgesic ω-conotoxins from the vermivorous cone snail <i>Conus moncuri</i> provide new insights into the evolution of conopeptides","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-06-01 01:31:53.721589","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2018,"MonPub":null,"DateUpdate":"2018-09-25","DateCreate":"2018-09-25","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000444022800001","VABBcode":null,"OpenAcc":1,"DOI":"10.1038/s41598-018-31245-4"},"refs":null,"anarec":{"AnaID":301544,"PubliDate":2018,"Pagination":"15 pp","XtraPublOfAnaID":null,"ISBN":null,"Volume":"8","Issue":"1","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":208093,"SerRR":"Scientific Reports (Nature Publishing Group). 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