title: Towards an understanding of Mesocestoides vogae fatty acid binding proteins' roles.
abstract: Two fatty acid binding proteins, MvFABPa and MvFABPb were identified in the parasite Mesocestoides vogae (Platyhelmithes, Cestoda). Fatty acid binding proteins are small intracellular proteins whose members exhibit great diversity. Proteins of this family have been identified in many organisms, of which Platyhelminthes are among the most primitive. These proteins have particular relevance in flatworms since de novo synthesis of fatty acids is absent. Fatty acids should be captured from the media needing an efficient transport system to uptake and distribute these molecules. While HLBPs could be involved in the shuttle of fatty acids to the surrounding host tissues and convey them into the parasite, FABPs could be responsible for the intracellular trafficking. In an effort to understand the role of MvFABPs in fatty acid transport of M. vogae larvae, we analysed the intracellular localization of both MvFABPs and the co-localization with in vivo uptake of fatty acid analogue BODIPY FL C16. Immunohistochemical studies on larvae sections using specific antibodies, showed a diffuse cytoplasmic distribution of each protein with some expression in nuclei and mitochondria. MvFABPs distribution was confirmed by mass spectrometry identification from 2D-electrophoresis of larvae subcellular fractions. This work is the first report showing intracellular distribution of MvFABPs as well as the co-localization of these proteins with the BODIPY FL C16 incorporated from the media. Our results suggest that fatty acid binding proteins could target fatty acids to cellular compartments including nuclei. In this sense, M. vogae FABPs could participate in several cellular processes fulfilling most of the functions attributed to vertebrate's counterparts.
authors.affiliation: Sección Bioquímica, Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay.
authors.forename: Gabriela
authors.initials: G
authors.lastname: Alvite
authors.affiliation: Sección Bioquímica, Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay.
authors.forename: Natalia
authors.initials: N
authors.lastname: Garrido
authors.affiliation: Sección Bioquímica, Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay; Instituto de Investigaciones Biológicas Clemente Estable, Montevideo, Uruguay.
authors.forename: Alejandra
authors.initials: A
authors.lastname: Kun
authors.affiliation: Centro de Bioinformática Estructural-DETEMA, Facultad de Química, Universidad de la República, Montevideo, Uruguay.
authors.forename: Margot
authors.initials: M
authors.lastname: Paulino
authors.affiliation: Sección Bioquímica, Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay.
authors.forename: Adriana
authors.initials: A
authors.lastname: Esteves
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D050556:Fatty Acid-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008645:Mesocestoides / Q000378:metabolism*; D008969:Molecular Sequence Data; D021381:Protein Transport
chemical_list: D050556:Fatty Acid-Binding Proteins; D015801:Helminth Proteins