{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T19:49:43Z","timestamp":1786736983202,"version":"build-2736575974"},"reference-count":34,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2008,5,1]]},"abstract":"<jats:p>Eight linear cationic peptides with cytolytic and insecticidal activity, designated cyto-insectotoxins (CITs), were identified in Lachesana tarabaevi spider venom. The peptides showed antibiotic activity towards Gram-positive and Gram-negative bacteria at micromolar concentrations as well as toxicity to insects. The primary structures of the toxins were established by direct Edman sequencing in combination with enzymatic and chemical polypeptide degradation and MS. CITs represent a novel class of cytolytic molecules and spider venom toxins. They are the first example of molecules showing equally potent antimicrobial and insecticidal effects. Analysis of L. tarabaevi venom gland expressed sequence tag database revealed the primary structures of the protein precursors; eight peptides homologous with the purified toxins were additionally predicted. CIT precursors share a conventional prepropeptide structure with an acidic prosequence and a processing motif common to most spider toxin precursors. The most abundant peptide, CIT 1a, was chemically synthesized, and its lytic activity on different bacterial strains, human erythrocytes and lymphocytes, insect cells, planar lipid bilayers and lipid vesicles was characterized. The spider L. tarabaevi is suggested to have evolved to rely on a unique set of linear cytolytic toxins, as opposed to the more common disulfide-containing spider neurotoxins.<\/jats:p>","DOI":"10.1042\/bj20071123","type":"journal-article","created":{"date-parts":[[2008,4,14]],"date-time":"2008-04-14T16:06:13Z","timestamp":1208189173000},"page":"687-696","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":61,"title":["Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom"],"prefix":"10.1042","volume":"411","author":[{"given":"Alexander\u00a0A.","family":"Vassilevski","sequence":"first","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergey\u00a0A.","family":"Kozlov","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olga\u00a0V.","family":"Samsonova","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalya\u00a0S.","family":"Egorova","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dmitry\u00a0V.","family":"Karpunin","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kirill\u00a0A.","family":"Pluzhnikov","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexei\u00a0V.","family":"Feofanov","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eugene\u00a0V.","family":"Grishin","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2008,4,14]]},"reference":[{"key":"2021112214143854600_B1","doi-asserted-by":"crossref","first-page":"2651","DOI":"10.1007\/s00018-003-3106-8","article-title":"Antimicrobial and cytolytic peptides of venomous arthropods","volume":"60","author":"Kuhn-Nentwig","year":"2003","journal-title":"Cell. Mol. Life Sci."},{"key":"2021112214143854600_B2","doi-asserted-by":"crossref","first-page":"20983","DOI":"10.1074\/jbc.M602168200","article-title":"Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity","volume":"281","author":"Kozlov","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2021112214143854600_B3","doi-asserted-by":"crossref","first-page":"2409","DOI":"10.1007\/s00018-003-3108-6","article-title":"Pharmacologically active spider peptide toxins","volume":"60","author":"Corzo","year":"2003","journal-title":"Cell. Mol. Life Sci."},{"key":"2021112214143854600_B4","doi-asserted-by":"crossref","first-page":"23627","DOI":"10.1074\/jbc.M200511200","article-title":"Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins","volume":"277","author":"Corzo","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2021112214143854600_B5","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1007\/s11030-006-9050-4","article-title":"Molecular diversification in spider venoms: a web of combinatorial peptide libraries","volume":"10","author":"Escoubas","year":"2006","journal-title":"Mol. Divers."},{"key":"2021112214143854600_B6","doi-asserted-by":"crossref","first-page":"2059","DOI":"10.1074\/jbc.273.4.2059","article-title":"Lycotoxins, antimicrobial peptides from venom of the wolf spider Lycosa carolinensis","volume":"273","author":"Yan","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2021112214143854600_B7","doi-asserted-by":"crossref","first-page":"11208","DOI":"10.1074\/jbc.M111099200","article-title":"Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae)","volume":"277","author":"Kuhn-Nentwig","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2021112214143854600_B8","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/0014-5793(73)80202-9","article-title":"Structure of melittin isolated from two species of honey bees","volume":"33","author":"Kreil","year":"1973","journal-title":"FEBS Lett."},{"key":"2021112214143854600_B9","doi-asserted-by":"crossref","first-page":"17823","DOI":"10.1074\/jbc.M100216200","article-title":"Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii","volume":"276","author":"Orivel","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021112214143854600_B10","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1021\/bi00504a006","article-title":"Estimation of globular protein secondary structure from circular dichroism","volume":"20","author":"Provencher","year":"1982","journal-title":"Biochemistry"},{"key":"2021112214143854600_B11","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1038\/194979a0","article-title":"Reconstitution of cell membrane structure in vitro and its transformation into an excitable system","volume":"194","author":"Mueller","year":"1962","journal-title":"Nature"},{"key":"2021112214143854600_B12","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/S0021-9258(18)64849-5","article-title":"A simple method for the isolation and purification of total lipides from animal tissues","volume":"226","author":"Folch","year":"1957","journal-title":"J. Biol. Chem."},{"key":"2021112214143854600_B13","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1002\/prot.20390","article-title":"A novel strategy for the identification of toxinlike structures in spider venom","volume":"59","author":"Kozlov","year":"2005","journal-title":"Proteins"},{"key":"2021112214143854600_B14","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.toxicon.2003.11.021","article-title":"Characterisation of major peptides in \u2018jack jumper\u2019 ant venom by mass spectrometry","volume":"43","author":"Davies","year":"2004","journal-title":"Toxicon"},{"key":"2021112214143854600_B15","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0005-2736(99)00200-X","article-title":"Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by \u03b1-helical antimicrobial and cell non-selective membrane-lytic peptides","volume":"1462","author":"Shai","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112214143854600_B16","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1146\/annurev.bi.47.070178.001343","article-title":"Empirical predictions of protein conformation","volume":"47","author":"Chou","year":"1978","journal-title":"Annu. Rev. Biochem."},{"key":"2021112214143854600_B17","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/0022-2836(78)90297-8","article-title":"Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins","volume":"120","author":"Garnier","year":"1978","journal-title":"J. Mol. Biol."},{"key":"2021112214143854600_B18","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1002\/1097-0282(2000)55:1<4::AID-BIP30>3.0.CO;2-M","article-title":"Amphipathic, \u03b1-helical antimicrobial peptides","volume":"55","author":"Tossi","year":"2000","journal-title":"Biopolymers"},{"key":"2021112214143854600_B19","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0014-5793(00)01384-3","article-title":"Scorpine, an anti-malaria and anti-bacterial agent purified from scorpion venom","volume":"471","author":"Conde","year":"2000","journal-title":"FEBS Lett."},{"key":"2021112214143854600_B20","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1007\/s00018-004-4149-1","article-title":"The scorpine family of defensins: gene structure, alternative polyadenylation and fold recognition","volume":"61","author":"Zhu","year":"2004","journal-title":"Cell. Mol. Life Sci."},{"key":"2021112214143854600_B21","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/S0041-0101(01)00199-4","article-title":"Pharmacology and biochemistry of spider venoms","volume":"40","author":"Rash","year":"2002","journal-title":"Toxicon"},{"key":"2021112214143854600_B22","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1016\/j.toxicon.2006.01.018","article-title":"Venom landscapes: mining the complexity of spider venoms via a combined cDNA and mass spectrometric approach","volume":"47","author":"Escoubas","year":"2006","journal-title":"Toxicon"},{"key":"2021112214143854600_B23","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/j.toxicon.2004.02.007","article-title":"Tarantulas: eight-legged pharmacists and combinatorial chemists","volume":"43","author":"Escoubas","year":"2004","journal-title":"Toxicon"},{"key":"2021112214143854600_B24","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.peptides.2004.07.016","article-title":"Were arachnids the first to use combinatorial peptide libraries?","volume":"26","author":"Sollod","year":"2005","journal-title":"Peptides"},{"key":"2021112214143854600_B25","doi-asserted-by":"crossref","first-page":"1693","DOI":"10.1016\/S0041-0101(98)00162-7","article-title":"Black widow spider toxins: the present and the future","volume":"36","author":"Grishin","year":"1998","journal-title":"Toxicon"},{"key":"2021112214143854600_B26","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/j.toxicon.2004.02.003","article-title":"Targeting ionotropic receptors with polyamine-containing toxins","volume":"43","author":"Mellor","year":"2004","journal-title":"Toxicon"},{"key":"2021112214143854600_B27","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1002\/jms.577","article-title":"De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis","volume":"39","author":"Budnik","year":"2004","journal-title":"J. Mass Spectrom."},{"key":"2021112214143854600_B28","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1016\/S0021-9258(18)89611-9","article-title":"Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus","volume":"260","author":"Argiolas","year":"1985","journal-title":"J. Biol. Chem."},{"key":"2021112214143854600_B29","doi-asserted-by":"crossref","first-page":"10106","DOI":"10.1016\/S0021-9258(18)90935-X","article-title":"Isolation and characterization of two new peptides, mastoparan C and crabrolin, from the venom of the European hornet, Vespa crabro","volume":"259","author":"Argiolas","year":"1984","journal-title":"J. Biol. Chem."},{"key":"2021112214143854600_B30","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1111\/j.1432-1033.1974.tb03787.x","article-title":"The amino-acid sequence and carbohydrate content of phospholipase A2 from bee venom","volume":"48","author":"Shipolini","year":"1974","journal-title":"Eur. J. Biochem."},{"key":"2021112214143854600_B31","first-page":"31173","article-title":"Conus peptides: biodiversity-based discovery and exogenomics","volume":"281","author":"Olivera","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2021112214143854600_B32","doi-asserted-by":"crossref","first-page":"6820","DOI":"10.1073\/pnas.96.12.6820","article-title":"Molecular genetics of ecological diversification: duplication and rapid evolution of toxin genes of the venomous gastropod Conus","volume":"96","author":"Duda","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112214143854600_B33","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/j.toxicon.2005.11.013","article-title":"Genetic mechanisms of scorpion venom peptide diversification","volume":"47","author":"Zhijian","year":"2006","journal-title":"Toxicon"},{"key":"2021112214143854600_B34","doi-asserted-by":"crossref","first-page":"5605","DOI":"10.1073\/pnas.92.12.5605","article-title":"Accelerated evolution in the protein-coding regions is universal in crotalinae snake venom gland phospholipase A2 isozyme genes. Proc","volume":"92","author":"Nakashima","year":"1995","journal-title":"Natl. Acad. Sci. U.S.A."}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/411\/3\/687\/652697\/bj4110687.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/411\/3\/687\/652697\/bj4110687.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T16:58:42Z","timestamp":1637600322000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/411\/3\/687\/44766\/Cyto-insectotoxins-a-novel-class-of-cytolytic-and"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2008,4,14]]},"references-count":34,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2008,5,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20071123","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2008,4,14]]}}}