{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,25]],"date-time":"2026-03-25T18:22:56Z","timestamp":1774462976443,"version":"3.50.1"},"reference-count":38,"publisher":"Portland Press Ltd.","issue":"16","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2016,8,15]]},"abstract":"<jats:p>In the present study, we show that venom of the ant spider Lachesana tarabaevi is unique in terms of molecular composition and toxicity. Whereas venom of most spiders studied is rich in disulfide-containing neurotoxic peptides, L. tarabaevi relies on the production of linear (no disulfide bridges) cytolytic polypeptides. We performed full-scale peptidomic examination of L. tarabaevi venom supported by cDNA library analysis. As a result, we identified several dozen components, and a majority (\u223c80% of total venom protein) exhibited membrane-active properties. In total, 33 membrane-interacting polypeptides (length of 18\u201379 amino acid residues) comprise five major groups: repetitive polypeptide elements (Rpe), latarcins (Ltc), met-lysines (MLys), cyto-insectotoxins (CIT) and latartoxins (LtTx). Rpe are short (18 residues) amphiphilic molecules that are encoded by the same genes as antimicrobial peptides Ltc 4a and 4b. Isolation of Rpe confirms the validity of the iPQM (inverted processing quadruplet motif) proposed to mark the cleavage sites in spider toxin precursors that are processed into several mature chains. MLys (51 residues) present \u2018idealized\u2019 amphiphilicity when modelled in a helical wheel projection with sharply demarcated sectors of hydrophobic, cationic and anionic residues. Four families of CIT (61\u201379 residues) are the primary weapon of the spider, accounting for its venom toxicity. Toxins from the CIT 1 and 2 families have a modular structure consisting of two shorter Ltc-like peptides. We demonstrate that in CIT 1a, these two parts act in synergy when they are covalently linked. This finding supports the assumption that CIT have evolved through the joining of two shorter membrane-active peptides into one larger molecule.<\/jats:p>","DOI":"10.1042\/bcj20160436","type":"journal-article","created":{"date-parts":[[2016,6,11]],"date-time":"2016-06-11T03:53:34Z","timestamp":1465617214000},"page":"2495-2506","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":35,"title":["<i>Lachesana tarabaevi<\/i>, an expert in membrane-active toxins"],"prefix":"10.1042","volume":"473","author":[{"given":"Alexey\u00a0I.","family":"Kuzmenkov","sequence":"first","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria\u00a0Y.","family":"Sachkova","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sergey\u00a0I.","family":"Kovalchuk","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eugene\u00a0V.","family":"Grishin","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexander\u00a0A.","family":"Vassilevski","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2016,8,11]]},"reference":[{"key":"2021112216300666700_B1","doi-asserted-by":"publisher","first-page":"1505","DOI":"10.1134\/S0006297909130069","article-title":"Molecular diversity of spider venom","volume":"74","author":"Vassilevski","year":"2009","journal-title":"Biochemistry (Mosc.)"},{"key":"2021112216300666700_B2","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/B978-0-12-387668-3.00001-5","article-title":"Venom composition and strategies in spiders: is everything possible?","volume":"40","author":"Kuhn-Nentwig","year":"2011","journal-title":"Adv. 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