9
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Neurotoxin Merging: A Strategy Deployed by the Venom of the Spider Cupiennius salei to Potentiate Toxicity on Insects

      research-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          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.

          Related collections

          Most cited references30

          • Record: found
          • Abstract: found
          • Article: not found

          Comparative Protein Structure Modeling Using MODELLER.

          Comparative protein structure modeling predicts the three-dimensional structure of a given protein sequence (target) based primarily on its alignment to one or more proteins of known structure (templates). The prediction process consists of fold assignment, target-template alignment, model building, and model evaluation. This unit describes how to calculate comparative models using the program MODELLER and how to use the ModBase database of such models, and discusses all four steps of comparative modeling, frequently observed errors, and some applications. Modeling lactate dehydrogenase from Trichomonas vaginalis (TvLDH) is described as an example. The download and installation of the MODELLER software is also described. © 2016 by John Wiley & Sons, Inc.
            Bookmark
            • Record: found
            • Abstract: not found
            • Article: not found

            MicroScale Thermophoresis: Interaction analysis and beyond

              Bookmark
              • Record: found
              • Abstract: not found
              • Article: not found

              Three-dimensional structure of membrane and surface proteins.

                Bookmark

                Author and article information

                Journal
                Toxins (Basel)
                Toxins (Basel)
                toxins
                Toxins
                MDPI
                2072-6651
                12 April 2020
                April 2020
                : 12
                : 4
                : 250
                Affiliations
                [1 ]Department of Nephrology and Hypertension, Inselspital, Bern University Hospital, Freiburgstrasse 15, 3010 Bern, Switzerland
                [2 ]Institute of Ecology and Evolution, University of Bern, Baltzerstrasse 6, 3012 Bern, Switzerland; nicolas.langenegger@ 123456iee.unibe.ch (N.L.); lukas.kopp@ 123456gmail.com (L.K.); wolfgang.nentwig@ 123456iee.unibe.ch (W.N.)
                [3 ]Toxicology and Pharmacology, University of Leuven (KU Leuven), Campus Gasthuisberg, O & N 2, Herestraat 49, P.O. Box 922, 3000 Leuven, Belgium; steve.peigneur@ 123456kuleuven.be
                [4 ]National Institutes of Health, Bethesda, MD 20892, USA; l_beni@ 123456hotmail.com
                Author notes
                [†]

                B.C. and L.K.-N. contributed equally to this work.

                Author information
                https://orcid.org/0000-0003-0504-5702
                Article
                toxins-12-00250
                10.3390/toxins12040250
                7232441
                32290562
                76484138-0aae-46f2-a43c-f9a4d25655fd
                © 2020 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 12 March 2020
                : 10 April 2020
                Categories
                Article

                Molecular medicine
                neurotoxin merging,cupiennius salei,venom,cstx-13,microscale thermophoresis,bioassay

                Comments

                Comment on this article