{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T00:49:59Z","timestamp":1787014199808,"version":"build-2736575974"},"reference-count":44,"publisher":"Wiley","issue":"23","license":[{"start":{"date-parts":[[2013,11,20]],"date-time":"2013-11-20T00:00:00Z","timestamp":1384905600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2013,12]]},"abstract":"<jats:sec>\n                    <jats:label\/>\n                    <jats:p>\n                      In addition to the conventional neurotoxins and cytotoxins, venom of the lynx spider\n                      <jats:italic>Oxyopes\u00a0takobius<\/jats:italic>\n                      was found to contain two\u2010domain modular toxins named spiderines: OtTx1a, 1b, 2a and 2b. These toxins show both insecticidal activity (a median lethal dose against flesh fly larvae of 75\u00a0\u03bcg\u00b7g\n                      <jats:sup>\u22121<\/jats:sup>\n                      ) and potent antimicrobial effects (minimal inhibitory concentrations in the range 0.1\u201310\u00a0\u03bc\n                      <jats:sc>m<\/jats:sc>\n                      ). Full sequences of the purified spiderines were established by a combination of Edman degradation, mass spectrometry and c\n                      <jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content>\n                      cloning. They are relatively large molecules (~\u00a0110 residues, 12.0\u201312.5\u00a0kDa) and consist of two distinct modules separated by a short linker. The N\u2013terminal part (~\u00a040 residues) contains no cysteine residues, is highly cationic, forms amphipathic \u03b1\u2013helical structures in a membrane\u2010mimicking environment, and shows potent cytolytic effects on cells of various origins. The C\u2013terminal part (~\u00a060 residues) is disulfide\u2010rich (five S\u2013S bonds), and contains the inhibitor cystine knot (ICK\/knottin) signature. The N\u2013terminal part of spiderines is very similar to linear cytotoxic peptides found in various organisms, whereas the C\u2013terminal part corresponds to the usual spider neurotoxins. We synthesized the modules of OtTx1a and compared their activity to that of full\u2010length mature toxin produced recombinantly, highlighting the importance of the N\u2013terminal part, which retained full\u2010length toxin activity in both insecticidal and antimicrobial assays. The unique structure of spiderines completes the range of two\u2010domain spider toxins.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Database<\/jats:title>\n                    <jats:p>\n                      The protein sequences of the spiderines (OtTx) reported in this paper have been submitted to the UniProt Knowledgebase (UniProtKB) under accession numbers\n                      <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.uniprot.org\/uniprot\/P86716\">P86716<\/jats:ext-link>\n                      \u2013\n                      <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.uniprot.org\/uniprot\/P86719\">P86719<\/jats:ext-link>\n                      , and the nucleotide sequences encoding OtTx have been submitted to the GenBank under accession numbers\n                      <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ncbi.nlm.nih.gov\/protein\/JX134894\">JX134894<\/jats:ext-link>\n                      \u2013\n                      <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ncbi.nlm.nih.gov\/protein\/JX134897\">JX134897<\/jats:ext-link>\n                      .\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/febs.12547","type":"journal-article","created":{"date-parts":[[2013,10,11]],"date-time":"2013-10-11T21:44:54Z","timestamp":1381527894000},"page":"6247-6261","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":27,"title":["Spider toxins comprising disulfide\u2010rich and linear amphipathic domains: a new class of molecules identified in the lynx spider\n                    <i>Oxyopes\u00a0takobius<\/i>"],"prefix":"10.1111","volume":"280","author":[{"given":"Alexander A.","family":"Vassilevski","sequence":"first","affiliation":[{"name":"M.M. 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