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Nicotinic acetylcholine receptors are novel targets of APETx-like toxins from the sea anemone Heteractis magnifica
Kalina, R.S.; Kasheverov, I.E.; Koshelev, S.G.; Sintsova, O.V.; Peigneur, S.; Pinheiro-Junior, E.L.; Popov, R.S.; Chausova, V.; Monastyrnaya, M.M.; Dmitrenok, P.S.; Isaeva, M.P.; Tytgat, J.; Kozlov, S.A.; Kozlovskaya, E.P.; Leychenko, E.V.; Gladkikh, I.N. (2022). Nicotinic acetylcholine receptors are novel targets of APETx-like toxins from the sea anemone Heteractis magnifica. Toxins 14(10): 697. https://dx.doi.org/10.3390/toxins14100697
In: Toxins. Multidisciplinary Digital Publishing Institute (MDPI): Basel. e-ISSN 2072-6651
Peer reviewed article  
Beschikbaar in  Auteurs 
Trefwoorden
    Heteractis magnifica (Quoy & Gaimard, 1833) [WoRMS]
    Marien/Kust
Author keywords
    sea anemones; phylogeny; APETx-like toxins; nicotinic acetylcholine receptors; acid-sensing ion channels
Auteurs  Top 
  • Kalina, R.S.
  • Kasheverov, I.E.
  • Koshelev, S.G.
  • Sintsova, O.V.
  • Peigneur, S.
  • Pinheiro-Junior, E.L.
  • Popov, R.S.
  • Chausova, V.
  • Monastyrnaya, M.M.
  • Dmitrenok, P.S.
  • Isaeva, M.P.
  • Tytgat, J., meer
  • Kozlov, S.A.
  • Kozlovskaya, E.P.
  • Leychenko, E.V.
  • Gladkikh, I.N.
Abstract
    The nicotinic acetylcholine receptors (nAChRs) are prototypical ligand-gated ion channels, provide cholinergic signaling, and are modulated by various venom toxins and drugs in addition to neurotransmitters. Here, four APETx-like toxins, including two new toxins, named Hmg 1b-2 Metox and Hmg 1b-5, were isolated from the sea anemone Heteractis magnifica and characterized as novel nAChR ligands and acid-sensing ion channel (ASIC) modulators. All peptides competed with radiolabeled α-bungarotoxin for binding to Torpedo californica muscle-type and human α7 nAChRs. Hmg 1b-2 potentiated acetylcholine-elicited current in human α7 receptors expressed in Xenopus laevis oocytes. Moreover, the multigene family coding APETx-like peptides library from H. magnifica was described and in silico surface electrostatic potentials of novel peptides were analyzed. To explain the 100% identity of some peptide isoforms between H. magnifica and H. crispa, 18S rRNA, COI, and ITS analysis were performed. It has been shown that the sea anemones previously identified by morphology as H. crispa belong to the species H. magnifica.
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