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Genes and evolution of two‐domain toxins from lynx spider venom
Author(s) -
Sachkova Maria Y.,
Slavokhotova Anna A.,
Grishin Eugene V.,
Vassilevski Alexander A.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.01.018
Subject(s) - domain (mathematical analysis) , gene , computational biology , biology , spider , genetics , zoology , mathematics , mathematical analysis
Spiderines are comparatively long polypeptide toxins (∼110 residues) from lynx spiders (genus Oxyopes ). They are built of an N‐terminal linear cationic domain (∼40 residues) and a C‐terminal knottin domain (∼60 residues). The linear domain empowers spiderines with strong cytolytic activity. In the present work we report 16 novel spiderine sequences from Oxyopes takobius and Oxyopes lineatus classified into two subfamilies. Strikingly, negative selection acts on both linear and knottin domains. Genes encoding Oxyopes two‐domain toxins were sequenced and found to be intronless. We further discuss a possible scenario of lynx spider modular toxin evolution.