{"refrec":{"BRefID":307906,"RR":"<b>Orts, D.J.B.; Peigneur, S.; Silva-Goncalves, L.C.; Arcisio-Miranda, M.; Bicudo, J.E.P.W.; Tytgat, J.</b> (2018). AbeTx1 is a novel sea anemone toxin with a dual mechanism of action on Shaker-type K+ channels activation. <i>Mar. Drugs 16(10)</i>: 360. <a href=\"https://dx.doi.org/10.3390/md16100360\" target=\"_blank\">https://dx.doi.org/10.3390/md16100360</a>","BEntID":300232,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Mar. Drugs 16(10)</i>: 360. <a href=\"https://dx.doi.org/10.3390/md16100360\" target=\"_blank\">https://dx.doi.org/10.3390/md16100360</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Orts, D.J.B.; Peigneur, S.; Silva-Goncalves, L.C.; Arcisio-Miranda, M.; Bicudo, J.E.P.W.; Tytgat, J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Orts, D.J.B. <i>et al.</i>","Englishabstract":"Voltage-gated potassium (K<sub>V</sub>) channels regulate diverse physiological processes and are an important target for developing novel therapeutic approaches. Sea anemone (Cnidaria, Anthozoa) venoms comprise a highly complex mixture of peptide toxins with diverse and selective pharmacology on K<sub>V</sub> channels. From the nematocysts of the sea anemone <span class=\"html-italic\">Actinia bermudensis</span>, a peptide that we named AbeTx1 was purified and functionally characterized on 12 different subtypes of K<sub>V</sub> channels (K<sub>V</sub>1.1–K<sub>V</sub>1.6; K<sub>V</sub>2.1; K<sub>V</sub>3.1; K<sub>V</sub>4.2; K<sub>V</sub>4.3; K<sub>V</sub>11.1; and, Shaker IR), and three voltage-gated sodium channel isoforms (Na<sub>V</sub>1.2, Na<sub>V</sub>1.4, and BgNa<sub>V</sub>). AbeTx1 was selective for Shaker-related K<sup>+</sup> channels and is capable of inhibiting K<sup>+</sup> currents, not only by blocking the K<sup>+</sup> current of K<sub>V</sub>1.2 subtype, but by altering the energetics of activation of K<sub>V</sub>1.1 and K<sub>V</sub>1.6. Moreover, experiments using six synthetic alanine point-mutated analogs further showed that a ring of basic amino acids acts as a multipoint interaction for the binding of the toxin to the channel. The AbeTx1 primary sequence is composed of 17 amino acids with a high proportion of lysines and arginines, including two disulfide bridges (Cys1–Cys4 and Cys2–Cys3), and it is devoid of aromatic or aliphatic amino acids. Secondary structure analysis reveals that AbeTx1 has a highly flexible, random-coil-like conformation, but with a tendency of structuring in the beta sheet. Its overall structure is similar to open-ended cyclic peptides found on the scorpion κ-KTx toxins family, cone snail venoms, and antimicrobial peptides.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"AbeTx1 is a novel sea anemone toxin with a dual mechanism of action on Shaker-type K+ channels activation","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-20 01:32:31.327140","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"sea anemone neurotoxin; Actinia bermudensis; potassium channel; type 6K-V-toxins; Alanine point mutation","OtherDescriptors":null,"Notes":null,"AnaPub":2018,"MonPub":null,"DateUpdate":"2019-03-15","DateCreate":"2019-03-13","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000448819600018","VABBcode":null,"OpenAcc":1,"DOI":"10.3390/md16100360"},"refs":null,"anarec":{"AnaID":307906,"PubliDate":2018,"Pagination":"360","XtraPublOfAnaID":null,"ISBN":null,"Volume":"16","Issue":"10","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":113252,"SerRR":"Marine Drugs. Molecular Diversity Preservation International (MDPI): Basel.  ISSN 1660-3397; e-ISSN 1660-3397","StandardTitleSer":"Marine Drugs","ISSN":"1660-3397","AbbrevSer":"Mar. Drugs","StandardTitleMon":null,"StartPage":19,"Pages":null,"ToPubliDate":null,"BRefBibLvlCode":"S","SerNotes":null},"monrec":null,"serrec":null,"relations":null,"relationsRev":null,"addrec":null,"othpubs":null,"ownerships":null,"authors":[{"AutName":"Orts","Firstname":"Diego","Initials":"D.J.B.","Affiliation":null,"Discriminator":null,"CorporateFlag":0,"BEntID":300232,"AutID":368093,"OrderNr":1,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":null,"InsFSN":null,"ORCID":null,"PersID":null,"InsID":null},{"AutName":"Peigneur","Firstname":"Steve","Initials":"S.","Affiliation":"Toxicology and Pharmacology, University of Leuven (KU Leuven)","Discriminator":null,"CorporateFlag":0,"BEntID":300232,"AutID":223893,"OrderNr":2,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":null,"InsFSN":"KU Leuven; Departement Farmaceutische en Farmacologische Wetenschappen; Laboratorium voor Toxicologie en Farmacologie","ORCID":"0000-0003-0504-5702","PersID":27019,"InsID":492},{"AutName":"Silva-Goncalves","Firstname":"Laiz","Initials":"L.C.","Affiliation":null,"Discriminator":null,"CorporateFlag":0,"BEntID":300232,"AutID":368095,"OrderNr":3,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":null,"InsFSN":null,"ORCID":null,"PersID":null,"InsID":null},{"AutName":"Arcisio-Miranda","Firstname":"Manoel","Initials":"M.","Affiliation":null,"Discriminator":null,"CorporateFlag":0,"BEntID":300232,"AutID":368096,"OrderNr":4,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":null,"InsFSN":null,"ORCID":null,"PersID":null,"InsID":null},{"AutName":"Bicudo","Firstname":"José","Initials":"J.E.P.W.","Affiliation":null,"Discriminator":null,"CorporateFlag":0,"BEntID":300232,"AutID":368097,"OrderNr":5,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":null,"InsFSN":null,"ORCID":null,"PersID":null,"InsID":null},{"AutName":"Tytgat","Firstname":"Jan","Initials":"J.","Affiliation":"Toxicology and Pharmacology, University of Leuven (KU Leuven)","Discriminator":null,"CorporateFlag":0,"BEntID":300232,"AutID":223897,"OrderNr":6,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":null,"InsFSN":"KU Leuven; Departement Farmaceutische en Farmacologische Wetenschappen; Laboratorium voor Toxicologie en Farmacologie","ORCID":null,"PersID":717,"InsID":492}],"mapdetails":null,"datasets":null,"monographs":null,"monparts":null,"serparts":null,"BEntOpen":null,"BEntPrivate":null,"availability":[{"BInstID":326348,"LibID":36,"BRefID":307906,"EmbargoDate":null,"FullEmbargoDate":null,"PhysMedID":16,"hasOCRd":1,"ShelfLocCode":"326348","RFID":null,"PaidValue":null,"Medium":"Server","Description":"VLIZ Open Access","Acronym":"VLIZ","Library":"Vlaams Instituut voor de Zee","DutchTerm":"Open access","URL":null,"ClassifID":53,"Classification":"Open access","ReqLink":null,"ClassifTypID":1,"URLLocation":"https://www.vliz.be/imisdocs/publications/","SubDir":null,"InternalReq":0,"LoggedInReq":0,"Disclaimer":null,"DutchDisclaimer":null,"FileFormat":".pdf","FileDescr":"pdf","InsPub":1,"InsID":36,"FileFormID":6,"LendableFlag":1,"PublicFlag":1,"orderLib":"A","Notes":null,"AccConID":null,"AccessConstraint":null,"LicURL":null}],"litstyles":null,"thespers":null,"arch2discl":null,"SERpubls":[{"PublName":"Molecular Diversity Preservation International (MDPI)","City":"Basel"}],"MONpubls":null,"pictures":[],"thestermsPath":null,"thestermsASFA":null,"taxtermsASFA":[{"TaxTerm":"Actinia bermudensis"}],"geotermsASFA":null,"collections":[{"Collection":"OMA - Open Marien Archief","ShortName":"OMA"}],"conf":null,"proj":null,"Physdatasets":null,"spcols":{"222":{"SpName":"BMB - Belgische Mariene Bibliografie","SpColID":222,"ParSpColID":null,"TopParID":null,"ShortName":"BMB","URLLocation":null,"LibID":36,"OpenRepoFlag":null,"SpTypID":null,"TopParIDNotWebsite":null,"SpColPath":"BMB"},"221":{"SpName":"OMA - Open Marien Archief","SpColID":221,"ParSpColID":null,"TopParID":null,"ShortName":"OMA","URLLocation":null,"LibID":36,"OpenRepoFlag":1,"SpTypID":null,"TopParIDNotWebsite":null,"SpColPath":"OMA"}},"doi":null,"publs":null,"serparttypes":null,"monauthors":null,"MParts":null,"SParts":null,"hLibs":null,"langs":[{"BEntID":300232,"AbstractFlag":0,"LangID":15,"LangCode":"en","Lang":"English","DutchTerm":"Engels","LangCodeExtended":"eng"},{"BEntID":300232,"AbstractFlag":1,"LangID":15,"LangCode":"en","Lang":"English","DutchTerm":"Engels","LangCodeExtended":"eng"}],"urls":[{"URL":"https://dx.doi.org/10.3390/md16100360","externalID":"10.3390/md16100360","URLTypeCode":"DOI","URLID":74650,"URLTypID":13,"URLType":"DOI","URLPrefix":"http://dx.doi.org/"}],"thesterms":null,"taxterms":[{"TaxTerm":"Actinia bermudensis","AphiaID":283273,"TaxtID":47109}],"geoterms":null,"othterms":null,"asfacodes":null,"asfa2codes":null,"thestermsFRIS":null,"taxtermsFRIS":[{"TaxTerm":"Actinia bermudensis","DutchTerm":null,"AphiaID":283273,"TaxtID":47109}],"geotermsFRIS":null,"othtermsFRIS":null,"resmessage":"","complete":1,"sessions":{"newSesName":"Lyssens, Liesbeth, L.","newSesDate":{"date":"2019-03-13 21:54:37.417000","timezone_type":3,"timezone":"Europe/Brussels"},"updSesName":"Bouchti, Zohra, Z.","updSesDate":{"date":"2019-03-15 08:01:16.333000","timezone_type":3,"timezone":"Europe/Brussels"}}}