Evidence map›Paper›PMID 22613721›Full record

ArticleThe Journal of biological chemistry2012

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

Lucia Kuhn-Nentwig, Irina M Fedorova, Benjamin P Lüscher, Lukas S Kopp, Christian Trachsel, Johann Schaller, Xuan Lan Vu, Thomas Seebeck, Kathrin Streitberger, Wolfgang Nentwig and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.7field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. The journal of venomous animals and toxins including tropical diseases · 2024
    Article
  3. Review
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  5. Widow spiders in the New World: a review onThe journal of venomous animals and toxins including tropical diseases · 2021
    Article
  6. The journal of venomous animals and toxins including tropical diseases · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Latarcins: versatile spider venom peptides.Cellular and molecular life sciences : CMLS · 2015
    Review
  17. Article
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 2 institutions in 2 countries.

Lucia Kuhn-NentwigInstitute of Ecology and Evolution, University of Bern, Baltzerstrasse 6, CH-3012 Bern, Switzerland. lucia.kuhn@iee.unibe.ch
Irina M Fedorova
Benjamin P Lüscher
Lukas S Kopp
Christian Trachsel
Johann Schaller
Xuan Lan Vu
Thomas Seebeck
Kathrin Streitberger
Wolfgang Nentwig
Erwin Sigel
Lev G Magazanik
University of Bern · CHInstitute of Evolutionary Physiology and Biochemistry · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Evolution, MolecularAnimalsCalcium Channels, L-TypeCell MembraneDNA, ComplementaryDrosophila melanogasterEscherichia coliFemaleMuscle, SkeletalNeurotoxinsProtein Structure, TertiaryRana temporariaSpidersSpider VenomsXenopus laevisCalcium Channels, L-TypeCSTX-1, Cupiennius saleiDNA, ComplementaryNeurotoxinsSpider Venoms

Identifiers

PMID22613721
PMCPMC3408166
OpenAlexW2049027824

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.