New view on crotamine, a small basic polypeptide myotoxin from South American rattlesnake venom

Abstract

Crotamine is a toxin from the Crotalus durissus terrificus venom, composed of 42 amino acid residues and three disulfide bridges. It belongs to a toxin family previously called Small Basic Polypeptide Myotoxins (SBPM) whose members are widely distributed through the Crotalus snake venoms. Comparison of SBPM amino acid sequences shows high similarities. Crotamine induces skeletal muscle spasms, leading to spastic paralysis of the hind limbs of mice, by interacting with sodium channels on muscle cells. The crotamine gene with 1.8 kbp is organized into three exons, which are separated by a long phase-1 and short phase-2 introns and mapped to chromosome 2. The three-dimensional structure of crotamine was recently solved and shares a structural topology with other three disulfide bond-containing peptide similar to human β-defensins and scorpion Na + channel toxin. Novel biological activities have been reported, such as the capacity to penetrate undifferentiated cells, to localize in the nucleus, and to serve as a marker of actively proliferating living cells.