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Cited by 78Venomous Animal Envenomation and StudiesNicotinic Acetylcholine Receptors StudyBotulinum Toxin and Related Neurological Disorders

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Last decade update for three-finger toxins: Newly emerging structures and biological activities

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Utkin, Yuri N·2019·World Journal of Biological Chemistry
DOI 10.4331/wjbc.v10.i1.17PMC PMC6314878
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Abstract

snake family, their presence has also been detected in the venoms of snakes from other families. The first TFT, α-bungarotoxin, was discovered almost 50 years ago and has since been used widely as a specific marker of the α7 and muscle-type nicotinic acetylcholine receptors. To date, the number of TFT amino acid sequences deposited in the UniProt Knowledgebase free-access database is more than 700, and new members are being added constantly. Although structural variations among the TFTs are not numerous, several new structures have been discovered recently; these include the disulfide-bound dimers of TFTs and toxins with nonstandard pairing of disulfide bonds. New types of biological activities have also been demonstrated for the well-known TFTs, and research on this topic has become a hot topic of TFT studies. The classic TFTs α-bungarotoxin and α-cobratoxin, for example, have now been shown to inhibit ionotropic receptors of γ-aminobutyric acid, and some muscarinic toxins have been shown to interact with adrenoceptors. New, unexpected activities have been demonstrated for some TFTs as well, such as toxin interaction with interleukin or insulin receptors and even TFT-activated motility of sperm. This minireview provides a summarization of the data that has emerged in the last decade on the TFTs and their activities.

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Figure 1 Spatial structures of dimeric three-finger toxins. A: Homodimer of α-cobratoxin, Protein Data Bank Identification code (PDB ID): 4AEA; B: Irditoxin, PDB ID: 2H7Z; C: Haditoxin, PDB ID: 3HH7; D: κ-bungarotoxin, PDB ID: 1KBA. Disulfide bonds are shown in yellow. N and C indicate N- and C-terminus, respectively.
Figure 1 Spatial structures of dimeric three-finger toxins. A: Homodimer of α-cobratoxin, Protein Data Bank Identification code (PDB ID): 4AEA; B: Irditoxin, PDB ID: 2H7Z; C: Haditoxin, PDB ID: 3HH7; D: κ-bungarotoxin, PDB ID: 1KBA. Disulfide bonds are shown in yellow. N and C indicate N- and C-terminus, respectively.CC BY-NC · PubMed Central
Figure 2 Alignment of amino acid sequence of toxin Tx7335 with those of nonconventional toxins. Cysteine residues are marked in yellow. Black lines indicate the locations of the typical disulfide bond in nonconventional toxins; red line indicates the unusual disulfide bond 25-55 in Tx7335. 3NOJ_DENAN: Toxin Tx7335 from Dendroaspis angusticeps (Eastern green mamba); 3NOJ_BUNCA: Bucandin from Bungarus candidus (Malayan krait); 3NOJ6_DENJA: Toxin S6C6 from Dendroaspis jamesoni kaimosae (Eastern Jameson's mamba); 3NOJ_WALAE: Actiflagelin from Walterinnesia aegyptia (desert black snake).
Figure 2 Alignment of amino acid sequence of toxin Tx7335 with those of nonconventional toxins. Cysteine residues are marked in yellow. Black lines indicate the locations of the typical disulfide bond in nonconventional toxins; red line indicates the unusual disulfide bond 25-55 in Tx7335. 3NOJ_DENAN: Toxin Tx7335 from Dendroaspis angusticeps (Eastern green mamba); 3NOJ_BUNCA: Bucandin from Bungarus candidus (Malayan krait); 3NOJ6_DENJA: Toxin S6C6 from Dendroaspis jamesoni kaimosae (Eastern Jameson's mamba); 3NOJ_WALAE: Actiflagelin from Walterinnesia aegyptia (desert black snake).CC BY-NC · PubMed Central

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References 49 · Cited by 78

Research works printed but not linked: 49

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Metadata

Authors
Utkin, Y. N.
Affiliations
Institute of Bioorganic Chemistry (RU)
Corresponding author
Utkin, Yuri N
ORCID
Utkin, Yuri N
Venue
World Journal of Biological Chemistry
Publisher
Baishideng Publishing Group Inc.
Published
2019-01-07
Volume
10
Issue
1
Pages
17-27
ISSN
1949-8454 (ISSN-L)
DOI
10.4331/wjbc.v10.i1.17
PMC
PMC6314878
OpenAlex
W2905755315
Cited by
78
References
49
Citations by year
2026: 15 · 2025: 11 · 2024: 7 · 2023: 9 · 2022: 11 · 2021: 11 · 2020: 6 · 2019: 8
FWCI
0.88
Type
journal article
Language
en
Open access
Licence
cc-by-nc
Locations
  • World Journal of Biological Chemistry (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
Funders
Russian Foundation for Basic Research
Topics
  • Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Venomous Animal Envenomation and Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
  • Health Sciences › Medicine › Clinical Neurology › Botulinum Toxin and Related Neurological Disorders
Keywords
three-finger toxins, snake venom toxins, alpha-bungarotoxin, alpha-cobratoxin, nicotinic acetylcholine receptors, GABAA receptor, muscarinic receptors, adrenergic receptors, insulin receptor binding, sperm motility, toxin structure

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Utkin, Y. N. (2019). Last decade update for three-finger toxins: Newly emerging structures and biological activities. World Journal of Biological Chemistry. https://doi.org/10.4331/wjbc.v10.i1.17