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FEBS Lett. 2014 Mar 3;588(5):740-5. doi: 10.1016/j.febslet.2014.01.018. Epub 2014 Jan 23.

Genes and evolution of two-domain toxins from lynx spider venom.

Author information

1
M.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya, 117997 Moscow, Russian Federation. Electronic address: sachkovamasha@mail.ru.
2
M.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya, 117997 Moscow, Russian Federation; N.I. Vavilov Institute of General Genetics, Russian Academy of Sciences, 3 Gubkina, 119991 Moscow, Russian Federation.
3
M.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya, 117997 Moscow, Russian Federation.
4
M.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya, 117997 Moscow, Russian Federation. Electronic address: avas@ibch.ru.

Abstract

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.

KEYWORDS:

Inhibitor cystine knot (ICK); Molecular evolution; Spider venom gland; Toxin gene; cDNA library

PMID:
24462682
DOI:
10.1016/j.febslet.2014.01.018
[Indexed for MEDLINE]
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