CLONING AND CHARACTERIZATION OF A RIBOSOMAL-P PROTEIN FROM TAENIA-SOLIUM, THE ETIOLOGIC AGENT OF HUMAN CYSTICERCOSIS

A cDNA encoding the complete open reading frame of the Taenia solium a cidic ribosomal phosphoprotein P2 has been cloned. The 417 bp cDNA (ar pP2) was isolated from a T. solium cDNA expression library by PCR usin g P protein specific pimers. The ORF encodes a protein of 121 amino ac ids exhibiting 40-55% identity to mammalian, fungal, insect, and paras ite P2 proteins. The inferred molecular mass of the protein is 12,592 OF Daltons, similar to that reported fur other ribosomal P2 proteins. After subcloning and expression, the recombinant protein was purified by affinity chromatography under non-denaturing conditions and was sho wn to have a molecular mass of 15 kDa which is equivalent to the expec ted size of the full length recombinant fusion protein, comprising the 12.6 kDa arpP2 plus an additional 2 kDa for the N-terminal fusion pep tide incorporating the six histidine residues required for purificatio n. (C) 1996 Academic Press, Inc.