For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
11
views
26
references
 Top references
cited by
9
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      214
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: not found

      CSTX-13, a highly synergistically acting two-chain neurotoxic enhancer in the venom of the spider Cupiennius salei (Ctenidae).

      Read this article at

      ScienceOpenPublisherPMC
          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 survival of the spider Cupiennius salei depends on its hunting success, which largely relies on its immediately paralyzing multicomponent venom. Here, we report on the isolation and characterization of CSTX-13, a neurotoxic enhancer in the spider venom. De novo elucidation of the disulfide bridge pattern of CSTX-13 and the neurotoxin CSTX-1 by tandem MS revealed an identical arrangement. However, in contrast to CSTX-1, CSTX-13 is a two-chain peptide with two interchain and two intrachain disulfide bridges. Furthermore, the insecticidal activity of CSTX-13 is synergistically increased in the presence of K+ ions as well as of the cytolytic peptide cupiennin 1a. We demonstrated that the weakly neurotoxic CSTX-13 enhances the paralytic activity of the neurotoxin CSTX-1 by 65% when it is administered with the latter at its entirely nontoxic physiological concentration, which is 440 times below its LD50 concentration.

          Related collections

          Most cited references26

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

          The cystine knot structure of ion channel toxins and related polypeptides.

          Raymond S. Norton, Paul Pallaghy (1998)
          An increasing number of ion channel toxins and related polypeptides have been found to adopt a common structural motif designated the inhibitor cystine knot motif (Pallaghy P. K., Nielsen, K. J., Craik, D. J., Norton, R. S. (1994) A common structural motif incorporating a cystine knot and triple-stranded beta-sheet in toxic and inhibitory polypeptides. Protein Science 3, 1833-1839). These globular, disulfide-stabilized molecules come from phylogenetically diverse sources, including spiders, cone shells, plants and fungi, and have various functions, although many target voltage-gated ion-channels. The common motif consists of a cystine knot and a triple-stranded, anti-parallel beta-sheet. Examples of ion-channel toxins known to adopt this structure are the omega-conotoxins and omega-agatoxins, and, more recently, robustoxin, versutoxin and protein 5 from spiders, as well as kappa-conotoxin PVIIA and conotoxin GS from cone shells. The variations on the motif structure exemplified by these structures are described here. We also consider the sequences of several polypeptides that might adopt this fold, including SNX-325 from a spider, delta-conotoxin PVIA and the muO-conotoxins from cone shells, and various plant and fungal polypeptides. The interesting case of the two- and three-disulfide bridged binding domains of the cellobiohydrolases from the fungus Trichoderma reesei is also discussed. The compact and robust nature of this motif makes it an excellent scaffold for the design and engineering of novel polypeptides with enhanced activity against existing targets, or with activity against novel targets.
          Article 0 comments Cited 56 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Identification of two novel Drosophila melanogaster histamine-gated chloride channel subunits expressed in the eye.

            Birgit Hirschberg, Bob Zheng, D M Schmatz … (2002)
            Histamine has been shown to play a role in arthropod vision; it is the major neurotransmitter of arthropod photoreceptors. Histamine-gated chloride channels have been identified in insect optic lobes. We report the first isolation of cDNA clones encoding histamine-gated chloride channel subunits from the fruit fly Drosophila melanogaster. The encoded proteins, HisCl1 and HisCl2, share 60% amino acid identity with each other. The closest structural homologue is the human glycine alpha3 receptor, which shares 45 and 43% amino acid identity respectively. Northern hybridization analysis suggested that hisCl1 and hisCl2 mRNAs are predominantly expressed in the insect eye. Oocytes injected with in vitro transcribed RNA, encoding either HisCl1 or HisCl2, produced substantial chloride currents in response to histamine but not in response to GABA, glycine, and glutamate. The histamine sensitivity was similar to that observed in insect laminar neurons. Histamine-activated currents were not blocked by picrotoxinin, fipronil, strychnine, or the H2 antagonist cimetidine. Co-injection of both hisCl1 and hisCl2 RNAs resulted in expression of a histamine-gated chloride channel with increased sensitivity to histamine, demonstrating coassembly of the subunits. The insecticide ivermectin reversibly activated homomeric HisCl1 channels and, more potently, HisCl1 and HisCl2 heteromeric channels.
            Article 0 comments Cited 43 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Biochemistry, toxicology and ecology of the venom of the spider Cupiennius salei (Ctenidae).

              Wolfgang Nentwig, Lucia Kuhn-Nentwig, Johann Schaller (2004)
              The venom of Cupiennius salei consists of many low molecular compounds, nine neurotoxic acting peptides (CSTX), at least eight neurotoxic and cytolytic acting peptides (cupiennins), a highly active hyaluronidase, and several hitherto unidentified proteins. The structure of several peptides is given. A synergistic action between three main groups is proposed: injected into the prey tissue, the enzyme hyaluronidase acts as a spreading factor, thus, facilitating a better access of venom neurotoxins to their targets, cupiennins disturb cell membranes and influence cell excitability, through this augmenting the mere neurotoxic effect of CSTX-1 synergistically. The venom glands of an apocrine secretion type provide an average of 12 microl per milking (adult female). Venom sensitivity of arthropods differs between 0.001 and >20nl venom/mg insect. Regeneration time of an empty venom gland is approx. 2 weeks. Consequently, spiders may encounter situations in which they have to decide whether their limited venom storage is sufficient to kill a given prey item. Experiments are presented which show that C. salei knows the actual venom content of its venom glands. It injects no more venom than necessary. This coincides with an experimentally determined LD(50) value in harmless prey items, but C. salei injects more venom in aggressive or otherwise dangerous prey items (quantification of injected venom amounts by monoclonal antibodies). These results indicate that C. salei uses its venom as economically as possible and this supports our venom optimisation hypothesis.
              Article 0 comments Cited 26 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (iso-abbrev): Proc. Natl. Acad. Sci. U.S.A.
                Title: Proceedings of the National Academy of Sciences of the United States of America
                Publisher: Proceedings of the National Academy of Sciences
                ISSN: 0027-8424
                ISSN (Print): 0027-8424
                Publication date (Electronic): Aug 03 2004
                Volume: 101
                Issue: 31
                Affiliations
                [1 ] Zoological Institute, University of Bern, Baltzerstrasse 6, CH-3012 Bern, Switzerland.
                Article
                Publisher Item ID: 0402226101
                DOI: 10.1073/pnas.0402226101
                PMC ID: 509190
                PubMed ID: 15272079
                SO-VID: df110d7e-776c-4648-86de-4ba55e10b668
                History

                Data availability:

                Comments

                Comment on this article

                scite_

                Similar content214

                See all similar

                Cited by10

                See all cited by

                Most referenced authors367

                See all reference authors