Neurotoxic Peptides in the Multicomponent Venom of the Spider Cupiennius Salei Part I. Primary Structure of Neurotoxic Peptides in Relation to their Biological Function
| Autor: | Johann Schaller, Lucia Kuhn-Nentwig, Stefan Schürch, Urs Kämpfer, Jürg Mülier, Wolfgang Nentwig |
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| Jazyk: | German<br />English<br />French |
| Rok vydání: | 2001 |
| Předmět: | |
| Zdroj: | CHIMIA, Vol 55, Iss 12 (2001) |
| Druh dokumentu: | article |
| ISSN: | 0009-4293 2673-2424 |
| Popis: | Beside other components, spider venom contains neurotoxically acting peptides which predominantly target a variety of different ion channels within the spider's prey. From the multicomponent venom of Cupiennius salei 13 toxic peptides (CSTX-1 – CSTX-13) were purified by a combination of gel filtration, cation-exchange chromatography, and reverse-phase HPLC. The amino acid sequence of two important neurotoxic peptides, CSTX-1 (74 residues, 8352.6 Da) and CSTX-9 (68 residues, 7530.9 Da), as well as CSTX-2a (61 residues, 6865.7 Da), a truncated form of CSTX-1, were determined by Edman degradation. Sequence comparison of CSTX-1 with CSTX-9 revealed an identity of 53% as well as identical positions of all eight cysteine residues. CSTX-1 and CSTX-9 share the same disulphide bridge pattern linking CYS1–CYS4, CYS2–Cys5, CYS3–CYS3 and CYS6–CYS7, This disulphide bridge pattern is also found in other spider toxins such as agatoxins and curtatoxins. CSTX-1 and CSTX-9 belong to the family of the ion channel toxins containing the inhibitor cystine knot structural motif with the consensus sequence: CX3-7CX3-10CX0-7CX1-8CX4-20C. CSTX-2a and CSTX-9, lacking the lysine-rich C-terminal tail of CSTX-1, exhibit a much lower toxicity for Drosophila melanogaster than CSTX-1, providing good evidence for the direct involvement of this lysine-rich C-terminal tail in the toxicity of CSTX-1. |
| Databáze: | Directory of Open Access Journals |
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