New Insectotoxin from Tibellus Oblongus Spider Venom Presents Novel Adaptation of ICK Fold
2021
Yuliya Korolkova | Ekaterina Maleeva | Alexander Mikov | Anna Lobas | Elizaveta Solovyeva | Mikhail Gorshkov | Yaroslav Andreev | Steve Peigneur | Jan Tytgat | Fedor Kornilov | Vladislav Lushpa | Konstantin Mineev | Sergey Kozlov
The Tibellus oblongus spider is an active predator that does not spin webs and remains poorly investigated in terms of venom composition. Here, we present a new toxin, named Tbo-IT2, predicted by cDNA analysis of venom glands transcriptome. The presence of Tbo-IT2 in the venom was confirmed by proteomic analyses using the LC-MS and MS/MS techniques. The distinctive features of Tbo-IT2 are the low similarity of primary structure with known animal toxins and the unusual motif of 10 cysteine residues distribution. Recombinant Tbo-IT2 (rTbo-IT2), produced in E. coli using the thioredoxin fusion protein strategy, was structurally and functionally studied. rTbo-IT2 showed insecticidal activity on larvae of the housefly Musca domestica (LD100 200 &mu:g/g) and no activity on the panel of expressed neuronal receptors and ion channels. The spatial structure of the peptide was determined in a water solution by NMR spectroscopy. The Tbo-IT2 structure is a new example of evolutionary adaptation of a well-known inhibitor cystine knot (ICK) fold to 5 disulfide bonds configuration, which determines additional conformational stability and gives opportunities for insectotoxicity and probably some other interesting features.
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