{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T04:23:48Z","timestamp":1787027028910,"version":"build-2736575974"},"reference-count":34,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2022,1,14]],"date-time":"2022-01-14T00:00:00Z","timestamp":1642118400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Pharmacol."],"abstract":"<jats:p>\n                    Venoms from cone snails and arachnids are a rich source of peptide modulators of voltage-gated sodium (Na\n                    <jats:sub>V<\/jats:sub>\n                    ) channels, however relatively few venom-derived peptides with activity at the mammalian Na\n                    <jats:sub>V<\/jats:sub>\n                    1.8 subtype have been isolated. Here, we describe the discovery and functional characterisation of \u03b2-theraphotoxin-Eo1a, a peptide from the venom of the Tanzanian black and olive baboon tarantula\n                    <jats:italic>Encyocratella olivacea<\/jats:italic>\n                    that modulates Na\n                    <jats:sub>V<\/jats:sub>\n                    1.8. Eo1a is a 37-residue peptide that increases Na\n                    <jats:sub>V<\/jats:sub>\n                    1.8 peak current (EC\n                    <jats:sub>50<\/jats:sub>\n                    894 \u00b1 146\u00a0nM) and causes a large hyperpolarising shift in both the voltage-dependence of activation (\u0394V\n                    <jats:sub>50<\/jats:sub>\n                    \u201320.5 \u00b1 1.2\u00a0mV) and steady-state fast inactivation (\u0394V\n                    <jats:sub>50<\/jats:sub>\n                    \u201315.5 \u00b1 1.8\u00a0mV). At a concentration of 10\u00a0\u03bcM, Eo1a has varying effects on the peak current and channel gating of Na\n                    <jats:sub>V<\/jats:sub>\n                    1.1\u2013Na\n                    <jats:sub>V<\/jats:sub>\n                    1.7, although its activity is most pronounced at Na\n                    <jats:sub>V<\/jats:sub>\n                    1.8. Investigations into the binding site of Eo1a using Na\n                    <jats:sub>V<\/jats:sub>\n                    1.7\/Na\n                    <jats:sub>V<\/jats:sub>\n                    1.8 chimeras revealed a critical contribution of the DII S3-S4 extracellular loop of Na\n                    <jats:sub>V<\/jats:sub>\n                    1.8 to toxin activity. Results from this work may form the basis for future studies that lead to the rational design of spider venom-derived peptides with improved potency and selectivity at Na\n                    <jats:sub>V<\/jats:sub>\n                    1.8.\n                  <\/jats:p>","DOI":"10.3389\/fphar.2021.789570","type":"journal-article","created":{"date-parts":[[2022,1,14]],"date-time":"2022-01-14T00:43:29Z","timestamp":1642121009000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":9,"title":["The Tarantula Venom Peptide Eo1a Binds to the Domain II S3-S4 Extracellular Loop of Voltage-Gated Sodium Channel NaV1.8 to Enhance Activation"],"prefix":"10.3389","volume":"12","author":[{"given":"Jennifer R.","family":"Deuis","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lotten","family":"Ragnarsson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samuel D.","family":"Robinson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zoltan","family":"Dekan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lerena","family":"Chan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ai-Hua","family":"Jin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Poanna","family":"Tran","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kirsten L.","family":"McMahon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shengnan","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John N.","family":"Wood","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James J.","family":"Cox","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Glenn F.","family":"King","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Volker","family":"Herzig","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irina","family":"Vetter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2022,1,14]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1038\/379257a0","article-title":"A Tetrodotoxin-Resistant Voltage-Gated Sodium Channel Expressed by Sensory Neurons","volume":"379","author":"Akopian","year":"1996","journal-title":"Nature"},{"key":"B2","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1016\/j.tips.2009.12.007","article-title":"Targeting Voltage Sensors in Sodium Channels with Spider Toxins","volume":"31","author":"Bosmans","year":"2010","journal-title":"Trends Pharmacol. 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