Cloning and expression of a cysteine-rich venom protein from Trimeresurus mucrosquamatus (Taiwan habu)

A full-length cDNA for cysteine-rich venom protein (CRVP) was constructed by immunoscreening and 5'-rapid amplification of cDNA ends from a cDNA library of venom gland of Trimeresurus mucrosquamatus. The predicted CRVP consisted of 183 amino acid residues including a putative signal peptide of 21 residues, Northern blot hybridization suggested the tissue-specific expression in venom gland and its corresponding length of cDNA, The predicted amino acid sequence of CRVP was homologous to a rat epididymal metalloprotein and a lizard helothermine. Amino acid sequence analysis suggested that CRVP may be a venom metalloprotein targeted against ryanodine receptors and Ca2+ release, Moreover, CRVP expressed in Escherichia coli exhibited the same antigenicity as their native venom forms of T. mucrosquamatus. This is the first report in the cloning and expression of a CRVP from the venom gland of T, mucrosquamatus. (C) 1997 Elsevier Science.