A venom-derived neurotoxin, CsTx-1, from the spider Cupiennius salei exhibits cytolytic activities

Kuhn-Nentwig, Lucia; Fedorova, Irina M; Lüscher, Benjamin P; Kopp, Lukas; Trachsel, Christian; Schaller, Johann; Vu Nguyen, Xuan Lan; Seebeck, Thomas; Streitberger, Kathrin; Nentwig, Wolfgang; Sigel, Erwin; Magazanik, Lev G (2012). A venom-derived neurotoxin, CsTx-1, from the spider Cupiennius salei exhibits cytolytic activities. Journal of biological chemistry, 287(30), pp. 25640-25649. Bethesda, Md.: American Society for Biochemistry and Molecular Biology 10.1074/jbc.M112.339051

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CsTx-1, the main neurotoxic acting peptide in the venom of the spider Cupiennius salei, is composed of 74 amino acid residues, exhibits an inhibitory cysteine knot motif, and is further characterized by its highly cationic charged C terminus. Venom gland cDNA library analysis predicted a prepropeptide structure for CsTx-1 precursor. In the presence of trifluoroethanol, CsTx-1 and the long C-terminal part alone (CT1-long; Gly-45-Lys-74) exhibit an α-helical structure, as determined by CD measurements. CsTx-1 and CT1-long are insecticidal toward Drosophila flies and destroys Escherichia coli SBS 363 cells. CsTx-1 causes a stable and irreversible depolarization of insect larvae muscle cells and frog neuromuscular preparations, which seem to be receptor-independent. Furthermore, this membranolytic activity could be measured for Xenopus oocytes, in which CsTx-1 and CT1-long increase ion permeability non-specifically. These results support our assumption that the membranolytic activities of CsTx-1 are caused by its C-terminal tail, CT1-long. Together, CsTx-1 exhibits two different functions; as a neurotoxin it inhibits L-type Ca(2+) channels, and as a membranolytic peptide it destroys a variety of prokaryotic and eukaryotic cell membranes. Such a dualism is discussed as an important new mechanism for the evolution of spider venomous peptides.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry
08 Faculty of Science > Department of Biology > Institute of Cell Biology
08 Faculty of Science > Department of Biology > Institute of Ecology and Evolution (IEE) > Community Ecology
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Kuhn-Nentwig, Lucia; Lüscher, Benjamin; Kopp, Lukas; Trachsel, Christian; Schaller, Johann; Vu Nguyen, Xuan Lan; Seebeck, Thomas; Streitberger, Kathrin; Nentwig, Wolfgang and Sigel, Erwin

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry
500 Science > 590 Animals (Zoology)
500 Science > 580 Plants (Botany)

ISSN:

0021-9258

Publisher:

American Society for Biochemistry and Molecular Biology

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:37

Last Modified:

24 Mar 2014 04:01

Publisher DOI:

10.1074/jbc.M112.339051

PubMed ID:

22613721

Web of Science ID:

000306651700071

URI:

https://boris.unibe.ch/id/eprint/15042 (FactScience: 222196)

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