Open AccessVoltage-gated sodium channels are targets for toxins from the venom of the spider Heriaeus melloteei
Author(s) -
Anton Nikolsky,
Bert Billen,
Alexander A. Vassilevski,
Sergey Filkin,
Jan Tytgat,
Eugene V. Grishin
Publication year - 2009
Publication title -
biochemistry (moscow) supplement series a membrane and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.206
H-Index - 12
eISSN - 1990-7494
pISSN - 1990-7478
DOI - 10.1134/s1990747809030027
Subject(s) - venom , sodium channel , spider , spider toxin , thomisidae , chemistry , gene isoform , biology , biochemistry , sodium , receptor , zoology , gene , glutamate receptor , organic chemistry
Three novel peptides were isolated from the venom of the spider Heriaeus melloteei (Thomisidae) and characterized. The peptides named Hm-1, 2 and 3 blocked voltage-gated sodium channels at concentrations in the order of 100 nM. Activity of the purified peptides was investigated in sodium channel isoforms of mammals and insects. Hm-1 and 2 appeared to act as pore blockers, whereas Hm-3 modulated the channel activation process. The toxins described exhibit minor similarity with other known peptides and may therefore constitute new groups of sodium channel ligands.status: publishe
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