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A tale of toxin promiscuity: the versatile pharmacological effects of Hcr 1b-2 sea anemone peptide on voltage-gated ion channels
Pinheiro-Junior, E.L.; Kalina, R.; Gladkikh, I.; Leychenko, E.; Tytgat, J.; Peigneur, S. (2022). A tale of toxin promiscuity: the versatile pharmacological effects of Hcr 1b-2 sea anemone peptide on voltage-gated ion channels. Mar. Drugs 20(2): 147. https://dx.doi.org/10.3390/md20020147
In: Marine Drugs. Molecular Diversity Preservation International (MDPI): Basel. ISSN 1660-3397; e-ISSN 1660-3397, more
Peer reviewed article  

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Keywords
    Radianthus crispa (Hemprich & Ehrenberg in Ehrenberg, 1834) [WoRMS]
    Marine/Coastal
Author keywords
    Heteractis crispa; APETx-like peptides; sea anemone; ion channels

Authors  Top 
  • Pinheiro-Junior, E.L., more
  • Kalina, R.
  • Gladkikh, I.
  • Leychenko, E.
  • Tytgat, J., more
  • Peigneur, S., more

Abstract
    Sea anemones are a rich source of biologically active compounds. Among approximately 1100 species described so far, Heteractis crispa species, also known as sebae anemone, is native to the Indo-Pacific area. As part of its venom components, the Hcr 1b-2 peptide was first described as an ASIC1a and ASIC3 inhibitor. Using Xenopus laevis oocytes and the two-electrode voltage-clamp technique, in the present work we describe the remarkable lack of selectivity of this toxin. Besides the acid-sensing ion channels previously described, we identified 26 new targets of this peptide, comprising 14 voltage-gated potassium channels, 9 voltage-gated sodium channels, and 3 voltage-gated calcium channels. Among them, Hcr 1b-2 is the first sea anemone peptide described to interact with isoforms from the Kv7 family and T-type Cav channels. Taken together, the diversity of Hcr 1b-2 targets turns this toxin into an interesting tool to study different types of ion channels, as well as a prototype to develop new and more specific ion channel ligands.

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