Cloning and characterization of Taenia saginata paramyosin cDNA

• Published in: Parasitology research (1987) Vol. 91; no. 1; pp. 60 - 67
• Main Authors: FERRER, Elizabeth, MOYANO, Eva, PARKHOUSE, E, GARATE, Teresa, BENITEZ, Laura, GONZALEZ, Luis Miguel, BRYCE, Denise, FOSTER-CUEVAS, Mildred, DAVILA, Iris, MILAGROS CORTEZ, Maria, HARRISON, Leslie J. S, MICHAEL, R
• Format: Journal Article
• Language: English
• Published: Berlin Springer 01-09-2003
• Subjects: Amino Acid Sequence; Animals; Antibodies, Helminth - blood; Biological and medical sciences; Cattle; Cattle Diseases - immunology; Cattle Diseases - parasitology; Cloning, Molecular; Collagen - metabolism; Cysticercosis - immunology; Cysticercosis - parasitology; DNA, Complementary - genetics; Fundamental and applied biological sciences. Psychology; Host parasite relation; pathogenicity; Humans; Invertebrates; Molecular Sequence Data; Nemathelminthia. Plathelmintha; Rabbits; Sequence Alignment; Sequence Analysis, DNA; Swine; Taenia saginata - genetics; Taenia saginata - metabolism; Tropomyosin - chemistry; Tropomyosin - genetics; Tropomyosin - immunology; Host parasite relation; Antigenic determinant; Nucleotide sequence; Plathelmintha; Parasite; Teniasis; Parasitosis; Cestoda; Gene expression; Immunodominance; Helminthiasis; Cestode disease; Infection; Binding protein; Complementary DNA; Immunogenicity; Paramyosin; Collagen; Helmintha; Invertebrata; Molecular cloning; Taenia saginata
• ISSN: 0932-0113; 1432-1955
• DOI: 10.1007/s00436-003-0895-5

A lambdaZAP-express cDNA library of Taenia saginata metacestodes was constructed. Antibody screening yielded a clone with an insert of 3,408 bp, an open reading frame of 2,589 bp, a deduced sequence of 863 amino acid and a molecular mass of 98.89 kDa. Alignments of the predicted amino acid sequence showed identity with paramyosins from several species: 98.8% with Taenia solium, 96.3% with Echinococcus.granulosus and about 70% with Schistosoma spp. The insert was expressed and purified. A collagen binding assay was performed which showed that T. saginata GST-paramyosin retained this property in a dose-dependent manner. Problems were encountered due to high backgrounds in serological assays in the homologous T. saginata system. However, the recombinant paramyosin was recognized by antibodies present in 31.6% of sera from T. solium seropositive cysticercosis patients and 100% of the sera from acute cysticercosis patients. The immunodominant epitope was the carboxyl-terminal fragment of the molecule.