CARACTERIZACIÓN E INMUNOREACTIVIDAD DE LA PROTEÍNA ACÍDICA RIBOSOMAL P2β DE L. (V.) braziliensis

Introduction: The serologic diagnosis of leishmaniosis using total proteins shows cross reactions. The characterization of new Leishmania antigens will improve the use of serological tools for the diagnosis of this disease. Objetive: To characterizate a new antigen of Leishmania. Materials and methods: the T166-U19 bacteriophage was characterizated from a cDNA L. (V.) braziliensis library which reacted against pooled sera from patients with cutaneous and mucocutaneous leishmaniasis. The T166-U19 cDNA clone was subcloned in a pGEX plasmid, sequenced, and the recombinant protein was expressed. The reactivity of this recombinant protein was assessed by ELISA. Results: The T166-U19 cDNA clone contained a 318- bp open reading frame (ORF) encoding 105 amino acid residues which has 81,1%, 82,9% and 60,7% identity with L. (L.) infantum LiP, L.(L.) donovani P2, and T. cruzi P2, respectively. Furthermore, the recombinant protein showed low reactivity (50%) with sera from patients with Leishmaniasis and it has croos-reactivity against sera from patients with Chagas disease. Conclusion: the P2__acidic ribosomal protein of L. (V.) braziliensis has been characterized for the first time and it has shown low reactivity against sera from patient with leishmaniasis.