A. Vazquez et al., CLONING AND CHARACTERIZATION OF THE CDNAS ENCODING NA-SPECIFIC TOXIN-1 AND TOXIN-2 OF THE SCORPION CENTRUROIDES-NOXIUS HOFFMANN( CHANNEL), Toxicon, 33(9), 1995, pp. 1161-1170
Using a cDNA library prepared from venomous glands of the Mexican scor
pion Centruroides noxius Hoffmann the genes that encode toxins 1 and 2
were identified, cloned and sequenced. In view of the proposed mechan
ism for processing the mature peptides coded by these two genes, the c
orresponding peptide-toxins were sequenced de novo. Mass spectrometric
and H-1-NMR analyses of the C-terminal peptide produced by enzymatic
digestion of both toxins indicated that the last residue is serine-ami
de. Sequence comparison revealed that these two genes have a similarit
y of 56% and 80% at the amino acid and nucleotide levels, respectively
. Small corrections to the published primary structures were introduce
d: Cn toxin 1 has an extra serine residue at position 65 and the resid
ue in position 60 is a proline, while the amino acids at positions 34
and 35 of Cn 2 are, respectively, tyrosine and glycine. Sequence compa
rison of toxins from the genus Centruroides suggests the presence of a
t least three classes of distinct peptides in these venoms.