{"refrec":{"BRefID":308017,"RR":"<b>Rodríguez, A.A.; Garateix, A.; Salceda, E.; Peigneur, S.; Zaharenko, A.J.; Pons, T.; Santos, Y.; Arreguin, R.; Ständker, L.; Forssmann, W.-G.; Tytgat, J.; Vega, R.; Soto, E.</b> (2018). PhcrTx2, a new crab-paralyzing peptide toxin from the sea anemone <i>Phymanthus crucifer</i>. <i>Toxins 10(2)</i>: 72. <a href=\"https://dx.doi.org/10.3390/toxins10020072\" target=\"_blank\">https://dx.doi.org/10.3390/toxins10020072</a>","BEntID":300343,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Toxins 10(2)</i>: 72. <a href=\"https://dx.doi.org/10.3390/toxins10020072\" target=\"_blank\">https://dx.doi.org/10.3390/toxins10020072</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Rodríguez, A.A.; Garateix, A.; Salceda, E.; Peigneur, S.; Zaharenko, A.J.; Pons, T.; Santos, Y.; Arreguin, R.; Ständker, L.; Forssmann, W.-G.; Tytgat, J.; Vega, R.; Soto, E.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Rodríguez, A.A. <i>et al.</i>","Englishabstract":"Sea anemones produce proteinaceous toxins for predation and defense, including peptide toxins that act on a large variety of ion channels of pharmacological and biomedical interest. <span class=\"html-italic\">Phymanthus crucifer</span> is commonly found in the Caribbean Sea; however, the chemical structure and biological activity of its toxins remain unknown, with the exception of PhcrTx1, an acid-sensing ion channel (ASIC) inhibitor. Therefore, in the present work, we focused on the isolation and characterization of new <span class=\"html-italic\">P. crucifer</span> toxins by chromatographic fractionation, followed by a toxicity screening on crabs, an evaluation of ion channels, and sequence analysis. Five groups of toxic chromatographic fractions were found, and a new paralyzing toxin was purified and named PhcrTx2. The toxin inhibited glutamate-gated currents in snail neurons (maximum inhibition of 35%, IC<sub>50</sub> 4.7 µM), and displayed little or no influence on voltage-sensitive sodium/potassium channels in snail and rat dorsal root ganglion (DRG) neurons, nor on a variety of cloned voltage-gated ion channels. The toxin sequence was fully elucidated by Edman degradation. PhcrTx2 is a new β-defensin-fold peptide that shares a sequence similarity to type 3 potassium channels toxins. However, its low activity on the evaluated ion channels suggests that its molecular target remains unknown. PhcrTx2 is the first known paralyzing toxin in the family Phymanthidae.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"PhcrTx2, a new crab-paralyzing peptide toxin from the sea anemone <i>Phymanthus crucifer</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; neutoxin; glutamate receptor; defensin-like fold; ionchannels; Phymanthus crucifer","OtherDescriptors":null,"Notes":null,"AnaPub":2018,"MonPub":null,"DateUpdate":"2019-03-19","DateCreate":"2019-03-13","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000427543800024","VABBcode":null,"OpenAcc":1,"DOI":"10.3390/toxins10020072"},"refs":null,"anarec":{"AnaID":308017,"PubliDate":2018,"Pagination":"72","XtraPublOfAnaID":null,"ISBN":null,"Volume":"10","Issue":"2","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":197331,"SerRR":"Toxins. 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