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Because of their high specificity, potency and stability, these peptides have attracted much attention as potential environmentally friendly insecticides. Although many insecticidal spider venom peptides have been isolated, the molecular target, mode of action and structure of only a small minority have been explored. Sf1a, a 46\u2010residue peptide isolated from the venom of the tube\u2010web spider <jats:italic>Segesteria\u00a0florentina<\/jats:italic>, is insecticidal to a wide range of insects, but nontoxic to vertebrates. In order to investigate its structure and mode of action, we developed an efficient bacterial expression system for the production of Sf1a. We determined a high\u2010resolution solution structure of Sf1a using multidimensional 3D\/4D <jats:styled-content style=\"fixed-case\">NMR<\/jats:styled-content> spectroscopy. This revealed that Sf1a is a knottin peptide with an unusually large \u03b2\u2010hairpin loop that accounts for a third of the peptide length. This loop is delimited by a fourth disulfide bond that is not commonly found in knottin peptides. We showed, through mutagenesis, that this large loop is functionally critical for insecticidal activity. Sf1a was further shown to be a selective inhibitor of insect voltage\u2010gated sodium channels, consistent with its \u2018depressant\u2019 paralytic phenotype in insects. However, in contrast to the majority of spider\u2010derived sodium channel toxins that function as gating modifiers via interaction with one or more of the voltage\u2010sensor domains, Sf1a appears to act as a pore blocker.<\/jats:p>","DOI":"10.1111\/febs.13189","type":"journal-article","created":{"date-parts":[[2015,1,5]],"date-time":"2015-01-05T14:51:18Z","timestamp":1420469478000},"page":"904-920","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":34,"title":["The insecticidal spider toxin <scp>SFI<\/scp>1 is a knottin peptide that blocks the pore of insect voltage\u2010gated sodium channels via a large \u03b2\u2010hairpin loop"],"prefix":"10.1111","volume":"282","author":[{"given":"Niraj S.","family":"Bende","sequence":"first","affiliation":[{"name":"Institute for Molecular Bioscience The University of Queensland St. Lucia Qld Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S\u0142awomir","family":"Dziemborowicz","sequence":"additional","affiliation":[{"name":"School of Medical &amp; Molecular Biosciences University of Technology Sydney NSW Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Volker","family":"Herzig","sequence":"additional","affiliation":[{"name":"Institute for Molecular Bioscience The University of Queensland St. Lucia Qld Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Venkatraman","family":"Ramanujam","sequence":"additional","affiliation":[{"name":"Centre for Advanced Imaging The University of Queensland St. Lucia Qld Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Geoffrey W.","family":"Brown","sequence":"additional","affiliation":[{"name":"Queensland Department of Agriculture Fisheries and Forestry Brisbane Qld Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Frank","family":"Bosmans","sequence":"additional","affiliation":[{"name":"Department of Physiology Johns Hopkins University Baltimore MA USA"},{"name":"Solomon H. 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