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http://purl.uniprot.org/citations/32290562http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32290562http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32290562http://www.w3.org/2000/01/rdf-schema#comment"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 Cupienniussalei venom."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.org/dc/terms/identifier"doi:10.3390/toxins12040250"xsd:string
http://purl.uniprot.org/citations/32290562http://purl.org/dc/terms/identifier"doi:10.3390/toxins12040250"xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Peigneur S."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Peigneur S."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Tytgat J."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Tytgat J."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Kuhn-Nentwig L."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Kuhn-Nentwig L."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Nentwig W."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Nentwig W."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Luescher B.P."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Luescher B.P."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Clemencon B."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Clemencon B."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Kopp L."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Kopp L."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Langenegger N."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/author"Langenegger N."xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/name"Toxins"xsd:string
http://purl.uniprot.org/citations/32290562http://purl.uniprot.org/core/name"Toxins"xsd:string