{"refrec":{"BRefID":338045,"RR":"<b>Kalina, R.S.; Peigneur, S.; Zelepuga, E.A.; Dmitrenok, P.S.; Kvetkina, A.N.; Kim, N.Y.; Leychenko, E.V.; Tytgat, J.; Kozlovskaya, E.P.; Monastyrnaya, M.M.; Gladkikh, I.N.</b> (2020). New insights into the type II toxins from the sea anemone <i>Heteractis crispa</i>. <i>Toxins 12(1)</i>: 44. <a href=\"https://hdl.handle.net/10.3390/toxins12010044\" target=\"_blank\">https://hdl.handle.net/10.3390/toxins12010044</a>","BEntID":334669,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Toxins 12(1)</i>: 44. <a href=\"https://hdl.handle.net/10.3390/toxins12010044\" target=\"_blank\">https://hdl.handle.net/10.3390/toxins12010044</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Kalina, R.S.; Peigneur, S.; Zelepuga, E.A.; Dmitrenok, P.S.; Kvetkina, A.N.; Kim, N.Y.; Leychenko, E.V.; Tytgat, J.; Kozlovskaya, E.P.; Monastyrnaya, M.M.; Gladkikh, I.N.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Kalina, R.S. <i>et al.</i>","Englishabstract":"Toxins modulating Na<sub>V</sub> channels are the most abundant and studied peptide components of sea anemone venom. Three type-II toxins, δ-SHTX-Hcr1f (= RpII), RTX-III, and RTX-VI, were isolated from the sea anemone <span class=\"html-italic\">Heteractis crispa</span>. RTX-VI has been found to be an unusual analog of RTX-III. The electrophysiological effects of <span class=\"html-italic\">Heteractis</span> toxins on nine Na<sub>V</sub> subtypes were investigated for the first time. <span class=\"html-italic\">Heteractis</span> toxins mainly affect the inactivation of the mammalian Na<sub>V</sub> channels expressed in the central nervous system (Na<sub>V</sub>1.1–Na<sub>V</sub>1.3, Na<sub>V</sub>1.6) as well as insect and arachnid channels (BgNa<sub>V</sub>1, VdNa<sub>V</sub>1). The absence of Arg13 in the RTX-VI structure does not prevent toxin binding with the channel but it has changed its pharmacological profile and potency. According to computer modeling data, the δ-SHTX-Hcr1f binds within the extracellular region of the rNa<sub>V</sub>1.2 voltage-sensing domain IV and pore-forming domain I through a network of strong interactions, and an additional fixation of the toxin at the channel binding site is carried out through the phospholipid environment. Our data suggest that <span class=\"html-italic\">Heteractis</span> toxins could be used as molecular tools for Na<sub>V</sub> channel studies or insecticides rather than as pharmacological agents.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"New insights into the type II toxins from the sea anemone <i>Heteractis crispa</i>","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"sea anemone; type II toxins; voltage-gated sodium channels; electrophysiology","OtherDescriptors":null,"Notes":null,"AnaPub":2020,"MonPub":null,"DateUpdate":"2021-05-30","DateCreate":"2021-05-17","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000514630000053","VABBcode":null,"OpenAcc":1,"Handle":"10.3390/toxins12010044"},"refs":null,"anarec":{"AnaID":338045,"PubliDate":2020,"Pagination":"44","XtraPublOfAnaID":null,"ISBN":null,"Volume":"12","Issue":"1","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":197331,"SerRR":"Toxins. 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