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 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.
Alvite
Gabriela
G
Biochemistry Section, Cellular and Molecular Biology Department, Faculty of Sciences, University of the Republic, Montevideo, Uruguay.
Canclini
Lucía
L
Corvo
Ileana
I
Esteves
Adriana
A
D000595:Amino Acid Sequence; D000818:Animals; D019143:Evolution, Molecular; D005091:Exons; D050556:Fatty Acid-Binding Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D015801:Helminth Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D007438:Introns; D008645:Mesocestoides / Q000378:metabolism*; D018613:Microscopy, Confocal; D008969:Molecular Sequence Data; D010802:Phylogeny; D016415:Sequence Alignment
D050556:Fatty Acid-Binding Proteins; D015801:Helminth Proteins