With the use of bioinformatic tools we identified an active domain of a novel cathepsin L-like cysteine protease (TsolCL) in the T. Subsequent catalytic cleavage of the pro-peptide converts these zymogens into enzymes. These proteases are expressed as zymogens which contain a signal peptide, pro-peptide, and an active domain. The cysteine protease family has previously been found to have important immunodiagnostic properties. In order to aid in the development of simple diagnostic approaches, identification and characterization of potential new antigens for immunodiagnostic purposes is desired. Porcine cysticercosis is an endemic parasitic disease caused by infection with Taenia solium that is found predominantly in developing countries. Universidad Peruana Cayetano Heredia, Av. Mirko Zimic, Laboratorio de Bioinformática y Biología Molecular. Pajuelo, Laboratorio de Bioinformática y Biología Molecular. Patricia Sheen, Laboratorio de Bioinformática y Biología Molecular. Lima, Peru.Īrmando Gonzales, School of Veterinary Medicine, Universidad Nacional Mayor de San Marcos, Av. García, Cysticercosis Unit, Instituto de Ciencias Neurológicas, Jirón Ancash 1271, Cercado de Lima 15003. Gilman, Department of International Health, Johns Hopkins Bloomberg School of Public Health, 615 North Wolfe Street, Baltimore, MD 21205, Maryland, USA.Ĭarlos Padilla, Laboratorio de Biotecnología y Biología molecular, Instituto Nacional de Salud, Cápac Yupanqui 1400 - Jesús María. Ruddy Liendo, Laboratorio de Bioinformática y Biología Molecular. Nancy León Janampa, Laboratorio de Bioinformática y Biología Molecular. solium metacestode was expressed successfully in Baculovirus system and was evaluated as a candidate antigen to diagnose porcine cysticercosis using the ELISA immunoassay. In conclusion, a novel cathepsin L-like cysteine protease from a T. Using ELISA, TsolCL was able to distinguish circulating IgG antibodies between healthy animals and naturally infected pigs with cysticercosis, showing a moderate sensitivity of 83.33% (40/48 95% CI: ), and a specificity of 83.78% (31/37 95% CI: ). In addition, TsolCL has cathepsin L conserved amino acid residues in the catalytic site (Gln8, Cys14, His159, Asn179 and Trp181) and the motif GCNGG. However, TsolCL was not able to hydrolyze human immunoglobulin. TsolCL showed cysteine protease enzymatic activity with the capacity to hydrolyze the Z-Phe-Arg-AMC substrate as well as bovine serum albumin. We cloned, expressed, purified, and characterized the recombinant active TsolCL (27 kDa) using the baculovirus-insect cell expression system. In addition, TsolCL was found to have a 61.9%-99.0% similarity to other cathepsin L proteins found in other helminths and mammals. Sequence alignment and phylogenetic analysis suggest that the TsolCL gene is closely related to genes found in Echinoccocus granulosus and E. The TsolCL gene includes 705 nucleotides (nt) within a single intron and a 633 nt exonic sequence encoding an active protein of 211 amino acids.
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