Purification and partial characterization of a 'short' insectotoxin-like peptide from the venom of the scorpion Parabuthus schlechteri.
A disulfide-rich, low-molecular-mass toxin-like peptide has been isolated from Parabuthus schlechteri venom using gel filtration, ion exchange, and reversed phase chromatography. Partial characterization of this peptide reveals a relationship with four-disulfide bridge proteins belonging to the family of 'short' insectotoxins (44% residue identity). In recognition hereof, the peptide was named PBITx1 (sITx10). Our work also reports on the deduced sequences of two other 'short' insectotoxins from Buthus eupeus, I3 and I4, and it provides a consensus sequence and nomenclature for all known 'short' insectotoxins. Finally, sequence similarities with K+ channel blockers (charybdotoxin, kappa-conotoxin), and a Cl- channel blocker (chlorotoxin) are highlighted.
Tytgat
J
J
Laboratory of Toxicology, University of Leuven, Belgium. jan.tytgat@farm.kuleuven.ac.be
Debont
T
T
Rostoll
K
K
Müller
G J
GJ
Verdonck
F
F
Daenens
P
P
van der Walt
J J
JJ
Possani
L D
LD
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D008969:Molecular Sequence Data; D012604:Scorpion Venoms / Q000737:chemistry* / Q000302:isolation & purification*; D017386:Sequence Homology, Amino Acid
C116854:PBITx1 protein, Parabuthus schlechteri; D012604:Scorpion Venoms