{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T22:15:31Z","timestamp":1777500931481,"version":"3.51.4"},"reference-count":47,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2016,10,15]],"date-time":"2016-10-15T00:00:00Z","timestamp":1476489600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["resjournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Insect Molecular Biology"],"published-print":{"date-parts":[[2017,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    <jats:italic>Loxosceles intermedia<\/jats:italic>\n                    venom comprises a complex mixture of proteins, glycoproteins and low molecular mass peptides that act synergistically to immobilize envenomed prey. Analysis of a venom\u2010gland transcriptome from\n                    <jats:italic>L. intermedia<\/jats:italic>\n                    revealed that knottins, also known as inhibitor cystine knot peptides, are the most abundant class of toxins expressed in this species. Knottin peptides contain a particular arrangement of intramolecular disulphide bonds, and these peptides typically act upon ion channels or receptors in the insect nervous system, triggering paralysis or other lethal effects. Herein, we focused on a knottin peptide with 53 amino acid residues from\n                    <jats:italic>L. intermedia<\/jats:italic>\n                    venom. The recombinant peptide, named U\n                    <jats:sub>2<\/jats:sub>\n                    \u2010sicaritoxin\u2010Li1b (Li1b), was obtained by expression in the periplasm of\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    . The recombinant peptide induced irreversible flaccid paralysis in sheep blowflies. We screened for knottin\u2010encoding sequences in total RNA extracts from two other\n                    <jats:italic>Loxosceles<\/jats:italic>\n                    species,\n                    <jats:italic>Loxosceles gaucho<\/jats:italic>\n                    and\n                    <jats:italic>Loxosceles laeta<\/jats:italic>\n                    , which revealed that knottin peptides constitute a conserved family of toxins in the\n                    <jats:italic>Loxosceles<\/jats:italic>\n                    genus. The insecticidal activity of U\n                    <jats:sub>2<\/jats:sub>\n                    \u2010SCTX\u2010Li1b, together with the large number of knottin peptides encoded in\n                    <jats:italic>Loxosceles<\/jats:italic>\n                    venom glands, suggests that studies of these venoms might facilitate future biotechnological applications of these toxins.\n                  <\/jats:p>","DOI":"10.1111\/imb.12268","type":"journal-article","created":{"date-parts":[[2016,10,15]],"date-time":"2016-10-15T05:36:45Z","timestamp":1476509805000},"page":"25-34","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Insecticidal activity of a recombinant knottin peptide from\n                    <i>Loxosceles intermedia<\/i>\n                    venom and recognition of these peptides as a conserved family in the genus"],"prefix":"10.1111","volume":"26","author":[{"given":"F. H.","family":"Matsubara","sequence":"first","affiliation":[{"name":"Department of Cell Biology Federal University of Parana Jardim das Am\u00e9ricas Curitiba Paran\u00e1 Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G. O.","family":"Meissner","sequence":"additional","affiliation":[{"name":"Department of Cell Biology Federal University of Parana Jardim das Am\u00e9ricas Curitiba Paran\u00e1 Brazil"},{"name":"Institute for Molecular Bioscience, The University of Queensland St. Lucia QLD Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"V.","family":"Herzig","sequence":"additional","affiliation":[{"name":"Institute for Molecular Bioscience, The University of Queensland St. Lucia QLD Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H. 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