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The venom of Cupiennius salei is composed of dozens of neurotoxins, with most of them supposed to act on ion channels. Some insecticidal monomeric neurotoxins contain an α-helical part besides their inhibitor cystine knot (ICK) motif (type 1). Other neurotoxins have, besides the ICK motif, an α-helical part of an open loop, resulting in a heterodimeric structure (type 2). Due to their low toxicity, it is difficult to understand the existence of type 2 peptides. Here, we show with the voltage clamp technique in oocytes of Xenopus laevis that a combined application of structural type 1 and type 2 neurotoxins has a much more pronounced cytolytic effect than each of the toxins alone. In biotests with Drosophila melanogaster, the combined effect of both neurotoxins was enhanced by 2 to 3 log units when compared to the components alone. Electrophysiological measurements of a type 2 peptide at 18 ion channel types, expressed in Xenopus laevis oocytes, showed no effect. Microscale thermophoresis data indicate a monomeric/heterodimeric peptide complex formation, thus a direct interaction between type 1 and type 2 peptides, leading to cell death. In conclusion, peptide mergers between both neurotoxins are the main cause for the high cytolytic activity of Cupiennius salei venom.
Benjamin Clémençon; Lucia Kuhn-Nentwig; Nicolas Langenegger; Lukas Kopp; Steve Peigneur; Jan Tytgat; Wolfgang Nentwig; Benjamin P. Lüscher. Neurotoxin Merging: A Strategy Deployed by the Venom of the Spider Cupiennius salei to Potentiate Toxicity on Insects. Toxins 2020, 12, 250 .
AMA StyleBenjamin Clémençon, Lucia Kuhn-Nentwig, Nicolas Langenegger, Lukas Kopp, Steve Peigneur, Jan Tytgat, Wolfgang Nentwig, Benjamin P. Lüscher. Neurotoxin Merging: A Strategy Deployed by the Venom of the Spider Cupiennius salei to Potentiate Toxicity on Insects. Toxins. 2020; 12 (4):250.
Chicago/Turabian StyleBenjamin Clémençon; Lucia Kuhn-Nentwig; Nicolas Langenegger; Lukas Kopp; Steve Peigneur; Jan Tytgat; Wolfgang Nentwig; Benjamin P. Lüscher. 2020. "Neurotoxin Merging: A Strategy Deployed by the Venom of the Spider Cupiennius salei to Potentiate Toxicity on Insects." Toxins 12, no. 4: 250.
This review gives an overview on the development of research on spider venoms with a focus on structure and function of venom components and techniques of analysis. Major venom component groups are small molecular mass compounds, antimicrobial (also called cytolytic, or cationic) peptides (only in some spider families), cysteine-rich (neurotoxic) peptides, and enzymes and proteins. Cysteine-rich peptides are reviewed with respect to various structural motifs, their targets (ion channels, membrane receptors), nomenclature, and molecular binding. We further describe the latest findings concerning the maturation of antimicrobial, and cysteine-rich peptides that are in most known cases expressed as propeptide-containing precursors. Today, venom research, increasingly employs transcriptomic and mass spectrometric techniques. Pros and cons of venom gland transcriptome analysis with Sanger, 454, and Illumina sequencing are discussed and an overview on so far published transcriptome studies is given. In this respect, we also discuss the only recently described cross contamination arising from multiplexing in Illumina sequencing and its possible impacts on venom studies. High throughput mass spectrometric analysis of venom proteomes (bottom-up, top-down) are reviewed.
Nicolas Langenegger; Wolfgang Nentwig; Lucia Kuhn-Nentwig. Spider Venom: Components, Modes of Action, and Novel Strategies in Transcriptomic and Proteomic Analyses. Toxins 2019, 11, 611 .
AMA StyleNicolas Langenegger, Wolfgang Nentwig, Lucia Kuhn-Nentwig. Spider Venom: Components, Modes of Action, and Novel Strategies in Transcriptomic and Proteomic Analyses. Toxins. 2019; 11 (10):611.
Chicago/Turabian StyleNicolas Langenegger; Wolfgang Nentwig; Lucia Kuhn-Nentwig. 2019. "Spider Venom: Components, Modes of Action, and Novel Strategies in Transcriptomic and Proteomic Analyses." Toxins 11, no. 10: 611.
Most knowledge of spider venom concerns neurotoxins acting on ion channels, whereas proteins and their significance for the envenomation process are neglected. The here presented comprehensive analysis of the venom gland transcriptome and proteome of Cupiennius salei focusses on proteins and cysteine-containing peptides and offers new insight into the structure and function of spider venom, here described as the dual prey-inactivation strategy. After venom injection, many enzymes and proteins, dominated by α-amylase, angiotensin-converting enzyme, and cysteine-rich secretory proteins, interact with main metabolic pathways, leading to a major disturbance of the cellular homeostasis. Hyaluronidase and cytolytic peptides destroy tissue and membranes, thus supporting the spread of other venom compounds. We detected 81 transcripts of neurotoxins from 13 peptide families, whereof two families comprise 93.7% of all cysteine-containing peptides. This raises the question of the importance of the other low-expressed peptide families. The identification of a venom gland-specific defensin-like peptide and an aga-toxin-like peptide in the hemocytes offers an important clue on the recruitment and neofunctionalization of body proteins and peptides as the origin of toxins.
Lucia Kuhn-Nentwig; Nicolas Langenegger; Manfred Heller; Dominique Koua; Wolfgang Nentwig. The Dual Prey-Inactivation Strategy of Spiders-In-Depth Venomic Analysis of Cupiennius salei. Toxins 2019, 11, 167 .
AMA StyleLucia Kuhn-Nentwig, Nicolas Langenegger, Manfred Heller, Dominique Koua, Wolfgang Nentwig. The Dual Prey-Inactivation Strategy of Spiders-In-Depth Venomic Analysis of Cupiennius salei. Toxins. 2019; 11 (3):167.
Chicago/Turabian StyleLucia Kuhn-Nentwig; Nicolas Langenegger; Manfred Heller; Dominique Koua; Wolfgang Nentwig. 2019. "The Dual Prey-Inactivation Strategy of Spiders-In-Depth Venomic Analysis of Cupiennius salei." Toxins 11, no. 3: 167.