title: Characterization and functional analysis of fatty acid binding protein from the carcinogenic liver fluke, Opisthorchis viverrini.
abstract: In the present study, the cDNA encoding FABP (Ov-FABP) was isolated from the adult stage of Opisthorchis viverrini and characterized. The Ov-FABP protein sequence (107 amino acids) was predicted to have a molecular mass of 12.26kDa and an isoelectric point (PI) of 6.82. This sequence had a high identity and similarity to Cs-FABP of the related opisthorchid Clonorchis sinensis. Multiple sequence alignment with FABPs from other parasitic flatworms and mammals showed a number of conserved amino acids including Phe34, Gly37, Glu38, Glu39,Val50, Iso62, Gly81, Ile84, Ser87and Arg101. In addition, the structure of Ov-FABP was predicted to have eleven β-sheets and one α-helix based on the known structures for FABPs from human (hL-FABP), rat and a schistosome. Phylogenetic analysis of amino acid sequence data revealed a close relationship of Ov-FABP with Cs-FABP and hL-FABP. Reverse transcription-PCR revealed that Ov-FABP was transcribed in the egg, metacercaria, juvenile and adult stages. The soluble form of recombinant Ov-FABP (rOv-FABP) was shown to specifically bind fatty acids, including oleic acid, palmitic acid and linoleic acid, as shown for other animals. Anti-serum against rOv-FABP (produced in mice) located the protein to parenchyma, egg, sucker musculature, testes and tegument of adult O. viverrini. Taken together, the findings suggest key functional roles for Ov-FABP in development, reproduction and/or host-parasite interactions.
authors.affiliation: College of Medicine and Public Health, Ubon Ratchathani University, Ubon Ratchathani, Thailand. Electronic address: jittiyawadee.s@ubu.ac.th.
authors.forename: Jittiyawadee
authors.initials: J
authors.lastname: Sripa
authors.affiliation: Department of Parasitology, Faculty of Medicine, Khon Kaen University, Khon Kaen, Thailand.
authors.forename: Thewarach
authors.initials: T
authors.lastname: Laha
authors.affiliation: Department of Pathology, Faculty of Medicine, Khon Kaen University, Khon Kaen, Thailand.
authors.forename: Banchob
authors.initials: B
authors.lastname: Sripa
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; D006790:Host-Parasite Interactions; D008297:Male; D051379:Mice; D009891:Opisthorchis / Q000235:genetics / Q000502:physiology*; D009928:Organ Specificity; D010802:Phylogeny; D016415:Sequence Alignment
chemical_list: D050556:Fatty Acid-Binding Proteins; D015801:Helminth Proteins
keywords: Fatty acid binding protein; Opisthorchis viverrini; Protein expression