IMIS | Flanders Marine Institute

Flanders Marine Institute

Platform for marine research


Publications | Institutes | Persons | Datasets | Projects | Maps
[ report an error in this record ]basket (0): add | show Print this page

PhcrTx2, a new crab-paralyzing peptide toxin from the sea anemone Phymanthus crucifer
Rodríguez, A.A.; Garateix, A.; Salceda, E.; Peigneur, S.; Zaharenko, A.J.; Pons, T.; Santos, Y.; Arreguin, R.; Ständker, L.; Forssmann, W.-G.; Tytgat, J.; Vega, R.; Soto, E. (2018). PhcrTx2, a new crab-paralyzing peptide toxin from the sea anemone Phymanthus crucifer. Toxins 10(2): 72.
In: Toxins. Multidisciplinary Digital Publishing Institute (MDPI): Basel. ISSN 2072-6651; e-ISSN 2072-6651, more
Peer reviewed article  

Available in  Authors 

    Phymanthus crucifer (Le Sueur, 1817) [WoRMS]
Author keywords
    sea anemone; neutoxin; glutamate receptor; defensin-like fold; ionchannels; Phymanthus crucifer

Authors  Top 
  • Rodríguez, A.A.
  • Garateix, A.
  • Salceda, E.
  • Peigneur, S., more
  • Zaharenko, A.J.
  • Pons, T.
  • Santos, Y.
  • Arreguin, R.
  • Ständker, L.
  • Forssmann, W.-G.
  • Tytgat, J., more
  • Vega, R.
  • Soto, E.

    Sea anemones produce proteinaceous toxins for predation and defense, including peptide toxins that act on a large variety of ion channels of pharmacological and biomedical interest. Phymanthus crucifer is commonly found in the Caribbean Sea; however, the chemical structure and biological activity of its toxins remain unknown, with the exception of PhcrTx1, an acid-sensing ion channel (ASIC) inhibitor. Therefore, in the present work, we focused on the isolation and characterization of new P. crucifer toxins by chromatographic fractionation, followed by a toxicity screening on crabs, an evaluation of ion channels, and sequence analysis. Five groups of toxic chromatographic fractions were found, and a new paralyzing toxin was purified and named PhcrTx2. The toxin inhibited glutamate-gated currents in snail neurons (maximum inhibition of 35%, IC50 4.7 µM), and displayed little or no influence on voltage-sensitive sodium/potassium channels in snail and rat dorsal root ganglion (DRG) neurons, nor on a variety of cloned voltage-gated ion channels. The toxin sequence was fully elucidated by Edman degradation. PhcrTx2 is a new β-defensin-fold peptide that shares a sequence similarity to type 3 potassium channels toxins. However, its low activity on the evaluated ion channels suggests that its molecular target remains unknown. PhcrTx2 is the first known paralyzing toxin in the family Phymanthidae.

All data in the Integrated Marine Information System (IMIS) is subject to the VLIZ privacy policy Top | Authors