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 (∼80% of total venom protein) exhibited membrane-active properties. In total, 33 membrane-interacting polypeptides (length of 18–79 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 ‘idealized’ amphiphilicity when modelled in a helical wheel projection with sharply demarcated sectors of hydrophobic, cationic and anionic residues. Four families of CIT (61–79 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.
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A schematic representation of the potential effect (in low intracellular Ca2+ conditions) of the Ca2+-binding, EF-hand-containing cytoskeletal protein EFhd2 on kinesin-mediated transport and actin dynamics in presynaptic compartments. For a detailed overview of the links between EFhd2 and neurodegeneration, see the review by Mielenz and Gunn-Moore in this issue (Volume 473, Issue 16, pages 2429–2437). - PDF Icon PDF LinkFront Matter
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Research Article|
August 11 2016
Lachesana tarabaevi, an expert in membrane-active toxins
Alexey I. Kuzmenkov;
Alexey I. Kuzmenkov
*Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia
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Maria Y. Sachkova;
Maria Y. Sachkova
*Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia
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Sergey I. Kovalchuk;
Sergey I. Kovalchuk
*Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia
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Eugene V. Grishin;
Eugene V. Grishin
*Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia
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Alexander A. Vassilevski
Alexander A. Vassilevski
1
*Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia
1To whom correspondence should be addressed (email avas@ibch.ru).
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Publisher: Portland Press Ltd
Received:
January 25 2016
Revision Received:
June 07 2016
Accepted:
June 09 2016
Accepted Manuscript online:
June 10 2016
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2016 The Author(s). published by Portland Press Limited on behalf of the Biochemical Society
2016
Biochem J (2016) 473 (16): 2495–2506.
Article history
Received:
January 25 2016
Revision Received:
June 07 2016
Accepted:
June 09 2016
Accepted Manuscript online:
June 10 2016
Citation
Alexey I. Kuzmenkov, Maria Y. Sachkova, Sergey I. Kovalchuk, Eugene V. Grishin, Alexander A. Vassilevski; Lachesana tarabaevi, an expert in membrane-active toxins. Biochem J 15 August 2016; 473 (16): 2495–2506. doi: https://doi.org/10.1042/BCJ20160436
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