tailieunhanh - Báo cáo khoa học: Two novel Mesocestoides vogae fatty acid binding proteins – functional and evolutionary implications

This work describes two new fatty acid binding proteins (FABPs) identified in the parasite platyhelminth Mesocestoides vogae(syn. corti). The corre-sponding polypeptide chains share 62% identical residues and overall 90% similarity according to clustalx default conditions. | ỊFEBS Journal Two novel Mesocestoides vogae fatty acid binding proteins - functional and evolutionary implications Gabriela Alvite Lucia Canclini Ileana Corvo and Adriana Esteves Biochemistry Section Cellular and Molecular Biology Department Faculty of Sciences University of the Republic Montevideo Uruguay Keywords fatty acid binding proteins introns Mesocestoides vogae parasites platyhelminths Correspondence A. Esteves Facultad de Ciencias Seccion Bioquimica Igua 4225 P3 Anexo Norte CP 11400 Montevideo Uruguay Fax 598 2 525 8617 Tel 598 2 525 2095 E-mail aesteves@ Database Nucleotide sequences have been submitted to the GenBank database under the accession numbers EF488508 MvFABPa mRNA EF488509 MvFABPb mRNA EF488510 MvFABPb gene and EF488511 MvFABPa gene Received 4 August 2007 revised 29 October 2007 accepted 5 November 2007 doi This work describes two new fatty acid binding proteins FABPs identified in the parasite platyhelminth Mesocestoides vogae syn. corti . The corresponding polypeptide chains share 62 identical residues and overall 90 similarity according to CLUSTALX default conditions. Compared with Cestoda FABPs these proteins share the highest similarity score with the Taenia solium protein. M. vogae FABPs are also phylogenetically related to the FABP3 FABP4 mammalian FABP subfamilies. The native proteins were purified by chromatographical procedures and apparent molecular mass and isoelectric point were determined. Immunolocalization studies determined the localization of the expression of these proteins in the larval form of the parasite. The genomic exon-intron organization of both genes is also reported and supports new insights on intron evolution. Consensus motifs involved in splicing were identified. Fatty acid binding proteins FABPs are small 1415 kDa cytosolic proteins that bind non-covalently to hydrophobic ligands mainly fatty acids. These proteins are members of the calycin superfamily which .