Structural and functional comparison of toxins from the venom of the scorpions Centruroides infamatus infamatus, centruroides limpidus limpidus and Centruroides noxius

Two novel toxins containing 66 amino acid residues each were isolated from the venom of the scorpions Centruroides infamatus infamatus and Centruroides limpidus limpidus, respectively. Their full amino acid sequences were determined. Comparison of primary structures showed that they share 97% simila...

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Bibliographic Details
Published in:Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 1996-02, Vol.113 (2), p.331-339
Main Authors: Dehesa-Dávila, Manuel, Ramfrez, Angelina N, Zamudio, Fernando Z, Gurrola-Briones, Georgina, Liévano, Arturo, Darszon, Alberto, Possani, Lourival D
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Binding, Competitive
Brain - metabolism
Buthidae
Centruroides infamatus
Centruroides limpidus
Centruroides noxius
Chromatography, Gel
Female
Mice
Molecular Sequence Data
Muscle, Skeletal - physiology
Na + channel
oocyte expression
Oocytes - drug effects
Oocytes - physiology
Rats
scorpion toxins
Scorpion Venoms - chemistry
Scorpion Venoms - isolation & purification
Scorpion Venoms - pharmacology
Scorpiones
Scorpions
Sequence Homology, Amino Acid
Sodium Channels - drug effects
Sodium Channels - physiology
Species Specificity
Synaptic Membranes - metabolism
Synaptosomes - metabolism
Xenopus laevis
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Summary:Two novel toxins containing 66 amino acid residues each were isolated from the venom of the scorpions Centruroides infamatus infamatus and Centruroides limpidus limpidus, respectively. Their full amino acid sequences were determined. Comparison of primary structures showed that they share 97% similarity among themselves and 83% to that of toxin 2 from Centruroides noxius. The three toxins studied compete with each other for the same binding sites on membranes prepared from rat brain synaptosomes, suggesting that they are all β-scorpion toxins. Toxin action was assayed into the μI-2 rat skeletal muscle Na + channel heterologously expressed into Xenopus oocytes. All three toxins block this Na + channel in a similar fashion, without affecting inactivation, and showed IC 50 values in the micromolar concentration range.
ISSN:1096-4959
0305-0491
1879-1107
DOI:10.1016/0305-0491(95)02031-4