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Molecules
2022 Oct 26;2721:. doi: 10.3390/molecules27217278.
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Purification and Characterization of Bot33: A Non-Toxic Peptide from the Venom of Buthus occitanus tunetanus Scorpion.
ElFessi R
,
Khamessi O
,
Srairi-Abid N
,
Sabatier JM
,
Tytgat J
,
Peigneur S
,
Kharrat R
.
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Scorpion venom is a rich source of promising therapeutic compounds, such as highly selective ion channel ligands with potent pharmacological effects. Bot33 is a new short polypeptide of 38 amino acid residues with six cysteines purified from the venom of the Buthus occitanus tunetanus scorpion. Bot33 has revealed less than 40% identity with other known alpha-KTx families. This peptide displayed a neutral amino acid (Leucine), in the position equivalent to lysine 27, described as essential for the interaction with Kv channels. Bot33 did not show any toxicity following i.c.v. injection until 2 µg/kg mouse body weight. Due to its very low venom concentration (0.24%), Bot33 was chemically synthesized. Unexpectedly, this peptide has been subjected to a screening on ion channels expressed in Xenopus laevis oocytes, and it was found that Bot33 has no effect on seven Kv channel subtypes. Interestingly, an in silico molecular docking study shows that the Leu27 prevents the interaction of Bot33 with the Kv1.3 channel. All our results indicate that Bot33 may have a different mode of action from other scorpion toxins, which will be interesting to elucidate.
Aiyar,
Topology of the pore-region of a K+ channel revealed by the NMR-derived structures of scorpion toxins.
1995, Pubmed
Aiyar,
Topology of the pore-region of a K+ channel revealed by the NMR-derived structures of scorpion toxins.
1995,
Pubmed
Altschul,
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.
1997,
Pubmed
Banerjee,
Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel.
2013,
Pubmed
Batista,
Two novel toxins from the Amazonian scorpion Tityus cambridgei that block Kv1.3 and Shaker B K(+)-channels with distinctly different affinities.
2002,
Pubmed
Ben Abderrazek,
Neutralizing Dromedary-Derived Nanobodies Against BotI-Like Toxin From the Most Hazardous Scorpion Venom in the Middle East and North Africa Region.
2022,
Pubmed
Bontems,
Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins.
1991,
Pubmed
Crest,
Kaliotoxin, a novel peptidyl inhibitor of neuronal BK-type Ca(2+)-activated K+ channels characterized from Androctonus mauretanicus mauretanicus venom.
1992,
Pubmed
Dauplais,
On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures.
1997,
Pubmed
El Ayeb,
Immunochemistry of scorpion alpha-neurotoxins. Determination of the antigenic site number and isolation of a highly enriched antibody specific to a single antigenic site of toxin II of Androctonus australis Hector.
1983,
Pubmed
ElFessi-Magouri,
Kbot55, purified from Buthus occitanus tunetanus venom, represents the first member of a novel α-KTx subfamily.
2016,
Pubmed
,
Xenbase
ElFessi-Magouri,
Characterization of Kbot21 Reveals Novel Side Chain Interactions of Scorpion Toxins Inhibiting Voltage-Gated Potassium Channels.
2015,
Pubmed
,
Xenbase
Galeotti,
Diphenhydramine-induced amnesia is mediated by Gi-protein activation.
2003,
Pubmed
Goldstein,
The charybdotoxin receptor of a Shaker K+ channel: peptide and channel residues mediating molecular recognition.
1994,
Pubmed
,
Xenbase
Gubič,
Discovery of KV 1.3 ion channel inhibitors: Medicinal chemistry approaches and challenges.
2021,
Pubmed
Khamessi,
RK1, the first very short peptide from Buthus occitanus tunetanus inhibits tumor cell migration, proliferation and angiogenesis.
2018,
Pubmed
Kharrat,
Molecular characterization, antigenicity and immunogenicity of anatoxic polymeric forms conferring protection against scorpion venoms.
1997,
Pubmed
Kozakov,
The ClusPro web server for protein-protein docking.
2017,
Pubmed
Liu,
Structures of wild-type and H451N mutant human lymphocyte potassium channel KV1.3.
2021,
Pubmed
Mejri,
BotIT6: a potent depressant insect toxin from Buthus occitanus tunetanus venom.
2003,
Pubmed
Merrifield,
Solid phase synthesis.
1986,
Pubmed
Miller,
An overview of the potassium channel family.
2000,
Pubmed
Mouhat,
The 'functional' dyad of scorpion toxin Pi1 is not itself a prerequisite for toxin binding to the voltage-gated Kv1.2 potassium channels.
2004,
Pubmed
,
Xenbase
Naseem,
Cm28, a scorpion toxin having a unique primary structure, inhibits KV1.2 and KV1.3 with high affinity.
2022,
Pubmed
Norton,
Enhancing the therapeutic potential of peptide toxins.
2017,
Pubmed
Park,
Interaction of charybdotoxin with permeant ions inside the pore of a K+ channel.
1992,
Pubmed
Peigneur,
Small cyclic sodium channel inhibitors.
2021,
Pubmed
,
Xenbase
Renisio,
Solution structure of BmKTX, a K+ blocker toxin from the Chinese scorpion Buthus Martensi.
2000,
Pubmed
Rodríguez de la Vega,
Mining on scorpion venom biodiversity.
2010,
Pubmed
Sali,
Comparative protein modelling by satisfaction of spatial restraints.
1993,
Pubmed
Seeliger,
Ligand docking and binding site analysis with PyMOL and Autodock/Vina.
2010,
Pubmed
Selisko,
Cobatoxins 1 and 2 from Centruroides noxius Hoffmann constitute a subfamily of potassium-channel-blocking scorpion toxins.
1998,
Pubmed
Shakkottai,
Design and characterization of a highly selective peptide inhibitor of the small conductance calcium-activated K+ channel, SkCa2.
2001,
Pubmed
Shen,
Statistical potential for assessment and prediction of protein structures.
2006,
Pubmed
Srairi-Abid,
Purification, characterization and molecular modelling of two toxin-like proteins from the Androctonus australis Hector venom.
2000,
Pubmed
Swartz,
The scorpion toxin and the potassium channel.
2013,
Pubmed
Tytgat,
A unified nomenclature for short-chain peptides isolated from scorpion venoms: alpha-KTx molecular subfamilies.
1999,
Pubmed
Varga,
The Kv1.3 K+ channel in the immune system and its "precision pharmacology" using peptide toxins.
2021,
Pubmed
Verdes,
From Mollusks to Medicine: A Venomics Approach for the Discovery and Characterization of Therapeutics from Terebridae Peptide Toxins.
2016,
Pubmed
Webb,
Comparative Protein Structure Modeling Using MODELLER.
2016,
Pubmed
Wulff,
Antibodies and venom peptides: new modalities for ion channels.
2019,
Pubmed
Xiang,
Plectasin, first animal toxin-like fungal defensin blocking potassium channels through recognizing channel pore region.
2015,
Pubmed
Zhu,
Experimental conversion of a defensin into a neurotoxin: implications for origin of toxic function.
2014,
Pubmed
,
Xenbase
