New Insectotoxin from Tibellus Oblongus Spider Venom Presents Novel Adaptation of ICK Fold
| Autor: | Fedor Kornilov, Steve Peigneur, Elizaveta M. Solovyeva, Jan Tytgat, Alexander Mikov, Konstantin S. Mineev, Sergey A. Kozlov, Anna A. Lobas, Ekaterina E. Maleeva, Yuliya V. Korolkova, Vladislav A. Lushpa, Mikhail V. Gorshkov, Yaroslav A. Andreev |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Proteomics
Protein Folding DNA Complementary Protein Conformation Health Toxicology and Mutagenesis proteome lcsh:Medicine Spider Venoms Venom Peptide Toxicology Article ICK fold 03 medical and health sciences 0302 clinical medicine Complementary DNA Houseflies Animals Amino Acid Sequence 030304 developmental biology chemistry.chemical_classification 0303 health sciences biology Base Sequence Tibellus oblongus Chemistry spider venom lcsh:R Protein primary structure Spiders biology.organism_classification Biochemistry Gene Expression Regulation Larva NMR structure Inhibitor cystine knot Thioredoxin Transcriptome insectotoxin transcriptome 030217 neurology & neurosurgery Cysteine |
| Zdroj: | Toxins Toxins, Vol 13, Iss 29, p 29 (2021) Volume 13 Issue 1 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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