{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T04:35:55Z","timestamp":1761712555345,"version":"build-2065373602"},"reference-count":60,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2018,4,11]],"date-time":"2018-04-11T00:00:00Z","timestamp":1523404800000},"content-version":"am","delay-in-days":365,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#am"},{"start":{"date-parts":[[2017,4,11]],"date-time":"2017-04-11T00:00:00Z","timestamp":1491868800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100012166","name":"National Basic Research Program of China","doi-asserted-by":"publisher","award":["2010CB529801"],"award-info":[{"award-number":["2010CB529801"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["31370783","31370817"],"award-info":[{"award-number":["31370783","31370817"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2017,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Voltage\u2010gated sodium channels (Na\n                    <jats:sub>V<\/jats:sub>\n                    s) are activated by transiting the voltage sensor from the deactivated to the activated state. The crystal structures of several bacterial Na\n                    <jats:sub>V<\/jats:sub>\n                    s have captured the voltage sensor module (VSM) in an activated state, but structure of the deactivated voltage sensor remains elusive. In this study, we sought to identify peptide toxins stabilizing the deactivated VSM of bacterial Na\n                    <jats:sub>V<\/jats:sub>\n                    s. We screened fractions from several venoms and characterized a cystine knot toxin called JZTx\u201027 from the venom of tarantula\n                    <jats:italic>Chilobrachys jingzhao<\/jats:italic>\n                    as a high\u2010affinity antagonist of the prokaryotic Na\n                    <jats:sub>V<\/jats:sub>\n                    s Ns\n                    <jats:sub>V<\/jats:sub>\n                    Ba (nonselective voltage\u2010gated\n                    <jats:italic>Bacillus alcalophilus<\/jats:italic>\n                    ) and NaChBac (bacterial sodium channel from\n                    <jats:italic>Bacillus halodurans<\/jats:italic>\n                    ) (IC\n                    <jats:sub>50<\/jats:sub>\n                    = 112 nM and 30 nM, respectively). JZTx\u201027 was more efficacious at weaker depolarizing voltages and significantly slowed the activation but accelerated the deactivation of Ns\n                    <jats:sub>V<\/jats:sub>\n                    Ba, whereas the local anesthetic drug lidocaine was shown to antagonize Ns\n                    <jats:sub>V<\/jats:sub>\n                    Ba without affecting channel gating. Mutation analysis confirmed that JZTx\u201027 bound to S3\u20134 linker of Ns\n                    <jats:sub>V<\/jats:sub>\n                    Ba, with F98 being the critical residue in determining toxin affinity. All electrophysiological data and\n                    <jats:italic>in silico<\/jats:italic>\n                    analysis suggested that JZTx\u201027 trapped VSM of Ns\n                    <jats:sub>V<\/jats:sub>\n                    Ba in one of the deactivated states. In mammalian Na\n                    <jats:sub>V<\/jats:sub>\n                    s, JZTx\u201027 preferably inhibited the inactivation of Na\n                    <jats:sub>V<\/jats:sub>\n                    1.5 by targeting the fourth transmembrane domain. To our knowledge, this is the first report of peptide antagonist for prokaryotic Na\n                    <jats:sub>V<\/jats:sub>\n                    s. More important, we proposed that JZTx\u201027 stabilized the Ns\n                    <jats:sub>V<\/jats:sub>\n                    Ba VSM in the deactivated state and may be used as a probe to determine the structure of the deactivated VSM of Na\n                    <jats:sub>V<\/jats:sub>\n                    s.\u2014Tang, C., Zhou, X., Nguyen, P. T., Zhang, Y., Hu, Z., Zhang, C., Yarov\u2010Yarovoy, V., DeCaen, P. G., Liang, S., Liu, Z. A novel tarantula toxin stabilizes the deactivated voltage sensor of bacterial sodium channel. FASEB J. 31, 3167\u20133178 (2017).\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.fasebj.org\">www.fasebj.org<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1096\/fj.201600882r","type":"journal-article","created":{"date-parts":[[2017,4,11]],"date-time":"2017-04-11T21:00:27Z","timestamp":1491944427000},"page":"3167-3178","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["A novel tarantula toxin stabilizes the deactivated voltage sensor of bacterial sodium channel"],"prefix":"10.1096","volume":"31","author":[{"given":"Cheng","family":"Tang","sequence":"first","affiliation":[{"name":"The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development College of Life Sciences Hunan Normal University Changsha China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xi","family":"Zhou","sequence":"additional","affiliation":[{"name":"The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development College of Life Sciences Hunan Normal University Changsha China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Phuong Tran","family":"Nguyen","sequence":"additional","affiliation":[{"name":"Department of Physiology and Membrane Biology University of California Davis Davis California USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yunxiao","family":"Zhang","sequence":"additional","affiliation":[{"name":"The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development College of Life Sciences Hunan Normal University Changsha China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhaotun","family":"Hu","sequence":"additional","affiliation":[{"name":"The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development College of Life Sciences Hunan Normal University Changsha China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Changxin","family":"Zhang","sequence":"additional","affiliation":[{"name":"The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development College of Life Sciences Hunan Normal University Changsha China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vladimir","family":"Yarov\u2010Yarovoy","sequence":"additional","affiliation":[{"name":"Department of Physiology and Membrane Biology University of California Davis Davis California USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paul G.","family":"DeCaen","sequence":"additional","affiliation":[{"name":"Department of Pharmacology Feinberg School of Medicine Northwestern University Chicago Illinois USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Songping","family":"Liang","sequence":"additional","affiliation":[{"name":"The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development College of Life Sciences Hunan Normal University Changsha China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhonghua","family":"Liu","sequence":"additional","affiliation":[{"name":"The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development College of Life Sciences Hunan Normal University Changsha 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