title: Taenia solium: identification and preliminary characterization of a lipid binding protein with homology to the SEC14 catalytic domain.
abstract: The objective of this work is to identify proteins of the human and porcine parasite, Taenia solium, which may be exploited for control of the parasite. Through screening a cDNA library of T. solium metacestodes, we have identified a novel Sec-14-like Taenia lipid-binding protein that may play an important role in membrane trafficking. The Sec14-like sequence is a single copy gene, encoding a putative polypeptide of 320 amino acids and 36.1 kDa (sec14Tsol protein). Secondary amino acid structural analysis suggested that the sec14Tsol protein might contain two distinct structural domains, an amino-terminal alpha-helix rich domain and a mixed alpha-helix/beta-stand carboxy-terminal zone, showing homology with the conserved SEC14 domain found in a great number of proteins that bind lipids, as the regulators of membrane trafficking between Golgi membrane bilayers. Significantly, therefore, in a phosphoinositide-binding assay, sec14Tsol purified recombinant protein specifically interacted with important lipid regulators of membrane trafficking, with a preference for PI(3)P(2), PI(3,4)P(2), PI(4,5)P(2) and phosphatidic acid. Moreover, the sec14Tsol protein was localized in the Golgi apparatus of transfected cells and in the spiral canal region of T. solium metacestode tegument. As sec14Tsol protein may play an important role in membrane trafficking, its demonstrated localisation in the intact parasite tegument suggests its involvement in the function of the tegument and thus perhaps interaction with the host.
authors.affiliation: Instituto de Salud Carlos III, Centro Nacional de Microbiología, Ctra Majadahonda Pozuelo Km 2,2, 28220, Majadahonda Madrid, Spain.
authors.forename: Estrella
authors.initials: E
authors.lastname: Montero
authors.forename: Luis Miguel
authors.initials: LM
authors.lastname: Gonzalez
authors.forename: Pedro
authors.initials: P
authors.lastname: Bonay
authors.forename: Gabriela
authors.initials: G
authors.lastname: Rosas
authors.forename: Beatriz
authors.initials: B
authors.lastname: Hernandez
authors.forename: Edda
authors.initials: E
authors.lastname: Sciutto
authors.forename: R Michael E
authors.initials: RM
authors.lastname: Parkhouse
authors.forename: Leslie J S
authors.initials: LJ
authors.lastname: Harrison
authors.forename: Miguel Angel
authors.initials: MA
authors.lastname: Morales
authors.forename: Teresa
authors.initials: T
authors.lastname: Garate
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003001:Cloning, Molecular; D018509:DNA, Helminth / Q000737:chemistry; D050556:Fatty Acid-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D005260:Female; D006056:Golgi Apparatus / Q000378:metabolism; D015801:Helminth Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D006801:Humans; D008969:Molecular Sequence Data; D010716:Phosphatidylinositols / Q000378:metabolism; D017433:Protein Structure, Secondary / Q000502:physiology; D011817:Rabbits; D017386:Sequence Homology, Amino Acid; D013552:Swine; D041201:Taenia solium / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D018509:DNA, Helminth; D050556:Fatty Acid-Binding Proteins; D015801:Helminth Proteins; D010716:Phosphatidylinositols