Cloning and characterization of a ribosomal P protein from Taenia solium, the aetiological agent of human cysticercosis

Abstract

A cDNA encoding the complete open reading frame of the Taenia solium acidic ribosomal phosphoprotein P2 has been cloned. The 417 bp cDNA (arpP2) was isolated from a T. solium cDNA expression library by PCR using P protein specific pimers. The ORF encodes a protein of 121 amino acids exhibiting 40-55% identity to mammalian, fungal, insect, and parasite P2 proteins. The inferred molecular mass of the protein is 12,592 Daltons, similar to that reported for other ribosomal P2 proteins. After subcloning and expression, the recombinant protein was purified by affinity chromatography under non-denaturing conditions and was shown to have a molecular mass of 15 kDa which is equivalent to the expected size of the full length recombinant fusion protein, comprising the 12.5 kDa arpP2 plus an additional 2 kDa for the N-terminal fusion peptide incorporating the six histidine residues required for purification.