Evidence for a new class of scorpion toxins active against K+ channels.
cDNAs encoding novel long-chain scorpion toxins (64 amino acid residues, including only six cysteines) were isolated from cDNA libraries produced from the venom glands of the scorpions Androctonus australis from Old World and Tityus serrulatus from New World. The encoded peptides were very similar to a recently identified toxin from T. serrulatus, which is active against the voltage-sensitive 'delayed-rectifier' potassium channel, but they were completely different from the long-chain and short-chain scorpion toxins already characterised. However, there was some sequence similarity (42%) between these new toxins, Aa TX Kbeta and Ts TX Kbeta, and scorpion defensins purified from the hemolymph of Buthidae scorpions Leiurus quinquestriatus and A. australis. Thus, according to a multiple sequence alignment using CLUSTAL, these new toxins seem to be related to the scorpion defensins.
Unité Mixte de Rechereche 6560 du Centre National de la Recherche Scientifique, Institut Fédératif de Recherche Jean Roche, Université de la Méditerranée, Faculté de Médecine Secteur Nord, Marseille, France.
C
C
Legros
B
B
Céard
P E
PE
Bougis
M F
MF
Martin-Eauclaire
D000595:Amino Acid Sequence; D001483:Base Sequence; D018076:DNA, Complementary; D004220:Disulfides / Q000737:chemistry; D008969:Molecular Sequence Data; D015221:Potassium Channels / Q000187:drug effects*; D012604:Scorpion Venoms / Q000737:chemistry / Q000494:pharmacology*; D017386:Sequence Homology, Amino Acid; D014118:Toxins, Biological / Q000737:chemistry / Q000494:pharmacology*
D018076:DNA, Complementary; D004220:Disulfides; D015221:Potassium Channels; D012604:Scorpion Venoms; D014118:Toxins, Biological