General Information of This Target
Target ID
BTDT10275
Target Name
Sodium channel
Target Bioclass
Transporter and channel
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N.A.
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Mu-scoloptoxin(03)-Ssm3a IC50
˜9 nM
[1]
 Toxin Info    Mu-theraphotoxin-Hhn1b 1 IC50
44.6 nM
[2- 9]
 Toxin Info    Mu-theraphotoxin-Hhn1b 2 IC50
44.6 nM
[2- 9]
 Toxin Info    Mu-theraphotoxin-Hhn1b 3 IC50
44.6 nM
[2- 9]
 Toxin Info    HwTx-I IC50
55 nM
[10- 21]
 Toxin Info    Beta-mammal toxin Css2 IC50
307 nM
[22- 31]
References
Ref 1 Chemical punch packed in venoms makes centipedes excellent predators. Mol Cell Proteomics. 2012 Sep;11(9):640-50. doi: 10.1074/mcp.M112.018853. Epub 2012 May 17.
Ref 2 Molecular diversification of peptide toxins from the tarantula Haplopelma hainanum (Ornithoctonus hainana) venom based on transcriptomic, peptidomic, and genomic analyses. J Proteome Res. 2010 May 7;9(5):2550-64. doi: 10.1021/pr1000016.
Ref 3 Isolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin-sensitive sodium channels from the Chinese bird spider Selenocosmia hainana. Cell Mol Life Sci. 2003 May;60(5):972-8. doi: 10.1007/s00018-003-2354-x.
Ref 4 Inhibition of neuronal tetrodotoxin-sensitive Na+ channels by two spider toxins: hainantoxin-III and hainantoxin-IV. Eur J Pharmacol. 2003 Sep 5;477(1):1-7. doi: 10.1016/s0014-2999(03)02190-3.
Ref 5 Inhibition of sodium channels in rat dorsal root ganglion neurons by Hainantoxin-IV, a novel spider toxin. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003 Jan;35(1):82-5.
Ref 6 Synthesis and oxidative refolding of hainantoxin-IV. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2002 Jul;34(4):516-9.
Ref 7 [Solid-phase synthesis and biological characterization of S12A-HNTX-IV and R29A-HNTX-IV: two mutants of hainantoxin-IV]. Sheng Wu Gong Cheng Xue Bao. 2005 Jan;21(1):92-6.
Ref 8 Gating modifier toxins isolated from spider venom: Modulation of voltage-gated sodium channels and the role of lipid membranes. J Biol Chem. 2018 Jun 8;293(23):9041-9052. doi: 10.1074/jbc.RA118.002553. Epub 2018 Apr 27.
Ref 9 Structure--activity relationships of hainantoxin-IV and structure determination of active and inactive sodium channel blockers. J Biol Chem. 2004 Sep 3;279(36):37734-40. doi: 10.1074/jbc.M405765200. Epub 2004 Jun 16.
Ref 10 cDNA sequence analysis of seven peptide toxins from the spider Selenocosmia huwena. Toxicon. 2003 Dec;42(7):715-23. doi: 10.1016/j.toxicon.2003.08.007.
Ref 11 Properties and amino acid sequence of huwentoxin-I, a neurotoxin purified from the venom of the Chinese bird spider Selenocosmia huwena. Toxicon. 1993 Aug;31(8):969-78. doi: 10.1016/0041-0101(93)90256-i.
Ref 12 Assignment of the three disulfide bridges of huwentoxin-I, a neurotoxin from the spider selenocosmia huwena. J Protein Chem. 1993 Dec;12(6):735-40. doi: 10.1007/BF01024931.
Ref 13 Blockade of neuromuscular transmission by huwentoxin-I, purified from the venom of the Chinese bird spider Selenocosmia huwena. Toxicon. 1997 Jan;35(1):39-45. doi: 10.1016/s0041-0101(96)00072-4.
Ref 14 [Chemical synthesis and characterization of R20A-HWTX-I, a mutant of huwentoxin-I with single residue replacement]. Sheng Wu Gong Cheng Xue Bao. 2000 Jul;16(4):490-4.
Ref 15 The presynaptic activity of huwentoxin-I, a neurotoxin from the venom of the chinese bird spider Selenocosmia huwena. Toxicon. 2000 Sep;38(9):1237-46. doi: 10.1016/s0041-0101(99)00224-x.
Ref 16 The effect of Huwentoxin-I on Ca(2+) channels in differentiated NG108-15 cells, a patch-clamp study. Toxicon. 2001 Apr;39(4):491-8. doi: 10.1016/s0041-0101(00)00150-1.
Ref 17 Antinociceptive effects of intrathecally administered huwentoxin-I, a selective N-type calcium channel blocker, in the formalin test in conscious rats. Toxicon. 2005 Jan;45(1):15-20. doi: 10.1016/j.toxicon.2004.08.018.
Ref 18 The cross channel activities of spider neurotoxin huwentoxin-I on rat dorsal root ganglion neurons. Biochem Biophys Res Commun. 2007 Jun 8;357(3):579-83. doi: 10.1016/j.bbrc.2007.02.168. Epub 2007 Apr 9.
Ref 19 Functional expression of spider neurotoxic peptide huwentoxin-I in E. coli. PLoS One. 2011;6(6):e21608. doi: 10.1371/journal.pone.0021608. Epub 2011 Jun 23.
Ref 20 Chemical Synthesis, Proper Folding, Na(v) Channel Selectivity Profile and Analgesic Properties of the Spider Peptide Phlotoxin 1. Toxins (Basel). 2019 Jun 21;11(6):367. doi: 10.3390/toxins11060367.
Ref 21 Proton nuclear magnetic resonance studies on huwentoxin-I from the venom of the spider Selenocosmia huwena: 2. Three-dimensional structure in solution. J Protein Chem. 1997 Aug;16(6):565-74. doi: 10.1023/a:1026314722607.
Ref 22 Purification and chemical and biological characterizations of seven toxins from the Mexican scorpion, Centruroides suffusus suffusus. J Biol Chem. 1987 Apr 5;262(10):4452-9.
Ref 23 Expression of functional recombinant scorpion beta-neurotoxin Css II in E. coli. Peptides. 2000 Jun;21(6):767-72. doi: 10.1016/s0196-9781(00)00206-0.
Ref 24 Four disulfide-bridged scorpion beta neurotoxin CssII: heterologous expression and proper folding in vitro. Biochim Biophys Acta. 2007 Aug;1770(8):1161-8. doi: 10.1016/j.bbagen.2007.04.006. Epub 2007 May 1.
Ref 25 Isolation and molecular cloning of beta-neurotoxins from the venom of the scorpion Centruroides suffusus suffusus. Toxicon. 2011 Apr;57(5):739-46. doi: 10.1016/j.toxicon.2011.02.006. Epub 2011 Feb 15.
Ref 26 Heterologous expressed toxic and non-toxic peptide variants of toxin CssII are capable to produce neutralizing antibodies against the venom of the scorpion Centruroides suffusus suffusus. Immunol Lett. 2009 Aug 15;125(2):93-9. doi: 10.1016/j.imlet.2009.06.001. Epub 2009 Jun 12.
Ref 27 Differential phospholipid binding by site 3 and site 4 toxins. Implications for structural variability between voltage-sensitive sodium channel domains. J Biol Chem. 2005 Mar 25;280(12):11127-33. doi: 10.1074/jbc.M412552200. Epub 2005 Jan 4.
Ref 28 Addition of positive charges at the C-terminal peptide region of CssII, a mammalian scorpion peptide toxin, improves its affinity for sodium channels Nav1.6. Peptides. 2011 Jan;32(1):75-9. doi: 10.1016/j.peptides.2010.11.001. Epub 2010 Nov 13.
Ref 29 Negative-shift activation, current reduction and resurgent currents induced by -toxins from Centruroides scorpions in sodium channels. Toxicon. 2012 Feb;59(2):283-93. doi: 10.1016/j.toxicon.2011.12.003. Epub 2011 Dec 16.
Ref 30 Generation of a Broadly Cross-Neutralizing Antibody Fragment against Several Mexican Scorpion Venoms. Toxins (Basel). 2019 Jan 10;11(1):32. doi: 10.3390/toxins11010032.
Ref 31 Solution structure of native and recombinant expressed toxin CssII from the venom of the scorpion Centruroides suffusus suffusus, and their effects on Nav1.5 sodium channels. Biochim Biophys Acta. 2012 Mar;1824(3):478-87. doi: 10.1016/j.bbapap.2012.01.003. Epub 2012 Jan 11.
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