Taenia solium: identification and preliminary characterization of a lipid binding protein with homology to the SEC14 catalytic domain.
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.
Montero
Estrella
E
Instituto de Salud Carlos III, Centro Nacional de Microbiología, Ctra Majadahonda Pozuelo Km 2,2, 28220, Majadahonda Madrid, Spain.
Gonzalez
Luis Miguel
LM
Bonay
Pedro
P
Rosas
Gabriela
G
Hernandez
Beatriz
B
Sciutto
Edda
E
Parkhouse
R Michael E
RM
Harrison
Leslie J S
LJ
Morales
Miguel Angel
MA
Garate
Teresa
T
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
D018509:DNA, Helminth; D050556:Fatty Acid-Binding Proteins; D015801:Helminth Proteins; D010716:Phosphatidylinositols