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Mar Drugs
2022 Feb 17;202:. doi: 10.3390/md20020147.
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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 EL
,
Kalina R
,
Gladkikh I
,
Leychenko E
,
Tytgat J
,
Peigneur S
.
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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.
2016/04761-4 São Paulo Research Foundation, 88881.186830/2018-01 Coordenação de Aperfeicoamento de Pessoal de Nível Superior, GOA4919N Research Foundation - Flanders, GOE7120N Research Foundation - Flanders, GOC2319N Research Foundation - Flanders, 12W7822N Research Foundation - Flanders, CELSA 17/047 KU Leuven, PDM/19/164 KU Leuven, 22-24-00912 Russian Science Foundation
Boldrini-França,
Beyond hemostasis: a snake venom serine protease with potassium channel blocking and potential antitumor activities.
2020, Pubmed
Boldrini-França,
Beyond hemostasis: a snake venom serine protease with potassium channel blocking and potential antitumor activities.
2020,
Pubmed
Bordon,
From Animal Poisons and Venoms to Medicines: Achievements, Challenges and Perspectives in Drug Discovery.
2020,
Pubmed
Chen,
Structural and functional diversity of acidic scorpion potassium channel toxins.
2012,
Pubmed
Cologna,
Investigation of the relationship between the structure and function of Ts2, a neurotoxin from Tityus serrulatus venom.
2012,
Pubmed
,
Xenbase
Cooper,
The sea anemone purine, caissarone: adenosine receptor antagonism.
1995,
Pubmed
Diochot,
APETx1, a new toxin from the sea anemone Anthopleura elegantissima, blocks voltage-gated human ether-a-go-go-related gene potassium channels.
2003,
Pubmed
Diochot,
A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid-sensitive channel in sensory neurons.
2004,
Pubmed
,
Xenbase
Ferreira Junior,
Peripheral 5-HT3 Receptors Are Involved in the Antinociceptive Effect of Bunodosine 391.
2017,
Pubmed
Ferrer,
Tamoxifen inhibition of kv7.2/kv7.3 channels.
2013,
Pubmed
Fu,
Discovery of novel peptide neurotoxins from sea anemone species.
2021,
Pubmed
Gladkikh,
Kunitz-Type Peptides from the Sea Anemone Heteractis crispa Demonstrate Potassium Channel Blocking and Anti-Inflammatory Activities.
2020,
Pubmed
,
Xenbase
Gutiérrez,
Snakebite envenoming.
2017,
Pubmed
Huang,
A Transcriptomic Survey of Ion Channel-Based Conotoxins in the Chinese Tubular Cone Snail (Conus betulinus).
2017,
Pubmed
Imbrici,
Therapeutic Approaches to Genetic Ion Channelopathies and Perspectives in Drug Discovery.
2016,
Pubmed
Jensen,
Understanding the molecular basis of toxin promiscuity: the analgesic sea anemone peptide APETx2 interacts with acid-sensing ion channel 3 and hERG channels via overlapping pharmacophores.
2014,
Pubmed
Kalina,
New APETx-like peptides from sea anemone Heteractis crispa modulate ASIC1a channels.
2018,
Pubmed
,
Xenbase
Kim,
Channelopathies.
2014,
Pubmed
Koren,
Gating mechanism of a cloned potassium channel expressed in frog oocytes and mammalian cells.
1990,
Pubmed
,
Xenbase
Kozlov,
Convenient nomenclature of cysteine-rich polypeptide toxins from sea anemones.
2012,
Pubmed
Kvetkina,
Deep-Sea Anemones Are Prospective Source of New Antimicrobial and Cytotoxic Compounds.
2021,
Pubmed
Landoulsi,
Subtype-selective activation of K(v)7 channels by AaTXKβ₂₋₆₄, a novel toxin variant from the Androctonus australis scorpion venom.
2013,
Pubmed
,
Xenbase
Lange,
Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR.
2006,
Pubmed
,
Xenbase
Leychenko,
Multigene Family of Pore-Forming Toxins from Sea Anemone Heteractis crispa.
2018,
Pubmed
Liu,
Modulation of neuronal sodium channels by the sea anemone peptide BDS-I.
2012,
Pubmed
Madio,
Sea Anemone Toxins: A Structural Overview.
2019,
Pubmed
Matsumura,
Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization.
2021,
Pubmed
Moreels,
APETx4, a Novel Sea Anemone Toxin and a Modulator of the Cancer-Relevant Potassium Channel KV10.1.
2017,
Pubmed
,
Xenbase
Napp,
Glycosylation of Eag1 (Kv10.1) potassium channels: intracellular trafficking and functional consequences.
2005,
Pubmed
,
Xenbase
Peigneur,
Phoneutria nigriventer Spider Toxin PnTx2-1 (δ-Ctenitoxin-Pn1a) Is a Modulator of Sodium Channel Gating.
2018,
Pubmed
,
Xenbase
Peigneur,
A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins.
2012,
Pubmed
,
Xenbase
Peroz,
Kv7.1 (KCNQ1) properties and channelopathies.
2008,
Pubmed
Pinheiro-Junior,
Towards toxin PEGylation: The example of rCollinein-1, a snake venom thrombin-like enzyme, as a PEGylated biopharmaceutical prototype.
2021,
Pubmed
,
Xenbase
Prentis,
Sea Anemones: Quiet Achievers in the Field of Peptide Toxins.
2018,
Pubmed
Razpotnik,
A new phospholipase A2 isolated from the sea anemone Urticina crassicornis - its primary structure and phylogenetic classification.
2010,
Pubmed
Rivera-Torres,
Discovery and characterisation of a novel toxin from Dendroaspis angusticeps, named Tx7335, that activates the potassium channel KcsA.
2016,
Pubmed
Santos,
Stabilization of the conductive conformation of a voltage-gated K+ (Kv) channel: the lid mechanism.
2013,
Pubmed
Whicher,
Structure of the voltage-gated K⁺ channel Eag1 reveals an alternative voltage sensing mechanism.
2016,
Pubmed
Wulff,
Voltage-gated potassium channels as therapeutic targets.
2009,
Pubmed
Yeung,
Modulation of Kv3 subfamily potassium currents by the sea anemone toxin BDS: significance for CNS and biophysical studies.
2005,
Pubmed
