Expression of schistosomal cathepsin l1 in Escherichia coli and evaluation of its protective capacity in an animal challenge

Schistosomes utilize proteinases to accomplish several activities such as tissue penetration, tissue digestion and evasion of host immune responses. Cathepsin L is a cysteine proteinase of the papain superfamily detected in their gut lumen which indicates that this enzyme contributes to the proteolysis of ingested hemoglobin. Due to the roles played in the schistosome biology, proteolytic enzymes are considered potential targets for developing and guiding antischistosomal therapies. In the present work, the cathepsin L1 cDNA coding of Schistosoma mansoni was cloned into the pAE vector that provides high-level expression of heterologous proteins in Escherichia coli. The recombinant protein was expressed as inclusion bodies, purified under denaturing conditions through nickel-charged chromatography and used for experimental animal vaccination. ELISA was performed with the pooled sera. Although this protein was shown to be immunogenic, mice immunized with three doses of recombinant protein plus aluminum hydroxide as adjuvant were not protected against S. mansoni infection.