The CAP (CRISP, antigen 5 and Pr-1) protein superfamily occur in a great variety of species. Cysteine-rich secretory proteins (CRISPs) are a subgroup of this superfamily that, like many other toxins, show potential in their biological and pharmaceutical functions. CRISPs are found in a wide variety of animal tissue and snake venoms, where they inhibit both potassium-induced smooth muscle contraction and cyclic nucleotide-gated channels. From the CRISPs studied, the few that have been functionally characterized were reported to exhibit a multitude of activities. However, many venom CRISPs have yet to be assigned specific functions.
Therefore, to explore the biological and pharmaceutical functions of venom CRISP, we cloned and characterized CRISP transcripts in the venom extracted from a Western diamondback rattlesnake (Crotalus atrox). The results obtained from this research would be supplemental for future attempts at unlocking the full potential of CRISPs.
