{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T23:39:38Z","timestamp":1773099578744,"version":"3.50.1"},"reference-count":45,"publisher":"Portland Press Ltd.","issue":"4","license":[{"start":{"date-parts":[[2019,7,26]],"date-time":"2019-07-26T00:00:00Z","timestamp":1564099200000},"content-version":"vor","delay-in-days":1823,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2014,8,1]]},"abstract":"<jats:p>Envenoming following scorpion sting is a common emergency in many parts of the world. During scorpion envenoming, highly toxic small polypeptides of the venom diffuse rapidly within the victim causing serious medical problems. The exploration of toxin structure-function relationship would benefit from the generation of soluble recombinant scorpion toxins in Escherichia coli. We developed an in\u00a0vitro wheat germ translation system for the expression of the highly toxic Aah (Androctonus australis hector)II protein that requires the proper formation of four disulphide bonds. Soluble, recombinant N-terminal GST (glutathione S-transferase)-tagged AahII toxin is obtained in this in\u00a0vitro translation system. After proteolytic removal of the GST-tag, purified rAahII (recombinant AahII) toxin, which contains two extra amino acids at its N terminal relative to the native AahII, is highly toxic after i.c.v. (intracerebroventricular) injection in Swiss mice. An LD50 (median lethal dose)-value of 10\u00a0ng (or 1.33\u00a0pmol), close to that of the native toxin (LD50 of 3\u00a0ng) indicates that the wheat germ in\u00a0vitro translation system produces properly folded and biological active rAahII. In addition, NbAahII10 (Androctonus australis hector nanobody 10), a camel single domain antibody fragment, raised against the native AahII toxin, recognizes its cognate conformational epitope on the recombinant toxin and neutralizes the toxicity of purified rAahII upon injection in mice.<\/jats:p>","DOI":"10.1042\/bsr20140050","type":"journal-article","created":{"date-parts":[[2014,6,16]],"date-time":"2014-06-16T13:54:51Z","timestamp":1402926891000},"update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Wheat germ<i>in\u00a0vitro<\/i>translation to produce one of the most toxic sodium channel specific toxins"],"prefix":"10.1042","volume":"34","author":[{"given":"Wael","family":"Gad","sequence":"first","affiliation":[{"name":"Brussels Center for Redox Biology, 1050 Brussels, Belgium"},{"name":"Structural Biology Research Center, VIB, 1050 Brussels, Belgium"},{"name":"Structural Biology Brussels Laboratory, Vrije Universiteit Brussel, 1050 Brussels, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rahma","family":"Ben-Abderrazek","sequence":"additional","affiliation":[{"name":"Laboratoire des Venins et Mol\u00e9cules Th\u00e9rapeutiques, Institut Pasteur de Tunis-Universit\u00e9 Tunis El Manar, Tunisia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Khadija","family":"Wahni","sequence":"additional","affiliation":[{"name":"Brussels Center for Redox Biology, 1050 Brussels, Belgium"},{"name":"Structural Biology Research Center, VIB, 1050 Brussels, Belgium"},{"name":"Structural Biology Brussels Laboratory, Vrije Universiteit Brussel, 1050 Brussels, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Didier","family":"Vertommen","sequence":"additional","affiliation":[{"name":"de Duve Institute, Universit\u00e9 Catholique de Louvain, 1200 Brussels, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Serge","family":"Muyldermans","sequence":"additional","affiliation":[{"name":"Structural Biology Research Center, VIB, 1050 Brussels, Belgium"},{"name":"Cellular and Molecular Immunology, Vrije Universiteit Brussel, 1050 Brussels, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Balkiss","family":"Bouhaouala-Zahar","sequence":"additional","affiliation":[{"name":"Laboratoire des Venins et Mol\u00e9cules Th\u00e9rapeutiques, Institut Pasteur de Tunis-Universit\u00e9 Tunis El Manar, Tunisia"},{"name":"Medical School of Tunis, University of Tunis El Manar, El Manar, Tunisia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joris","family":"Messens","sequence":"additional","affiliation":[{"name":"Brussels Center for Redox Biology, 1050 Brussels, Belgium"},{"name":"Structural Biology Research Center, VIB, 1050 Brussels, Belgium"},{"name":"Structural Biology Brussels Laboratory, Vrije Universiteit Brussel, 1050 Brussels, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2014,7,29]]},"reference":[{"key":"2021111619180378400_B1","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1016\/j.actatropica.2008.05.021","article-title":"Epidemiology of scorpionism: a global appraisal","volume":"107","author":"Chippaux","year":"2008","journal-title":"Acta Tropica"},{"key":"2021111619180378400_B2","doi-asserted-by":"publisher","first-page":"358","DOI":"10.2174\/187152811797200713","article-title":"Immunological aspects of scorpion toxins: current status and perspectives","volume":"10","author":"Bouhaouala-Zahar","year":"2011","journal-title":"Inflamm. 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