title: A comparative study of biochemical and immunological properties of triosephosphate isomerase from Taenia solium and Sus scrofa.
abstract: We produced the Taenia solium triosephosphate isomerase (TPI) in Escherichia coli and compared its biochemical and immunological properties with those of the commercial TPI from Sus scrofa. Taenia solium TPI is a homodimer composed of two 27-kDa monomers, with a specific activity of 5,683 U/mg and a Km value of 0.758, and S. scrofa TPI is also dimeric with similar monomeric molecular weight, specific activity of 4,227 U/mg, and a Km value of 0.51. The catalytic parameters for the isomerization of glyceraldehyde 3-phosphate, affinity between TPI monomers, and kinetic thermal denaturation and inactivation were similar for both enzymes. Anti-T. solium TPI antibodies cross-react weakly with Schistosoma mansoni TPI but do not cross-react with S. scrofa, human, or protozoan TPIs. These antibodies inhibited T. solium TPI activity but did not affect S. scrofa enzymatic activity. Immunizations with 1 microg of the T. solium TPI reduced 52% of cysticerci in a mouse-Taenia crassiceps model 1 mo after challenge. Our findings show that T. solium and S. scrofa TPIs possess similar biochemical and enzymatic properties but do not share immunological properties because anti-T. solium TPI antibodies did not recognize S. scrofa TPI. Inhibition of enzyme activity by anti-TPI antibodies suggests that they can be used as inhibitors of the enzyme.
authors.affiliation: Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de México, Edificio A, 2 Piso, Ciudad Universitaria, México DF 04510, México.
authors.forename: Lucía
authors.initials: L
authors.lastname: Jiménez
authors.forename: D Alejandro
authors.initials: DA
authors.lastname: Fernández-Velasco
authors.forename: Kaethe
authors.initials: K
authors.lastname: Willms
authors.forename: Abraham
authors.initials: A
authors.lastname: Landa
mesh_terms: D000818:Animals; D000909:Antibodies, Helminth / Q000276:immunology; D000947:Antigens, Helminth / Q000737:chemistry / Q000276:immunology; D015153:Blotting, Western; D002850:Chromatography, Gel; D002942:Circular Dichroism; D003551:Cysticercosis / Q000276:immunology / Q000517:prevention & control; D004195:Disease Models, Animal; D004591:Electrophoresis, Polyacrylamide Gel; D015801:Helminth Proteins / Q000737:chemistry / Q000276:immunology; D006358:Hot Temperature; D007106:Immune Sera / Q000276:immunology; D051379:Mice; D017510:Protein Folding; D011817:Rabbits; D011994:Recombinant Proteins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification; D013552:Swine / Q000378:metabolism*; D041201:Taenia solium / Q000201:enzymology*; D014305:Triose-Phosphate Isomerase / Q000737:chemistry* / Q000276:immunology* / Q000302:isolation & purification
chemical_list: D000909:Antibodies, Helminth; D000947:Antigens, Helminth; D015801:Helminth Proteins; D007106:Immune Sera; D011994:Recombinant Proteins; D014305:Triose-Phosphate Isomerase