title: Taenia crassiceps cysticerci: Characterization of the 14-kDa glycoprotein with homologies to antigens from Taenia solium cysticerci.
abstract: Glycoproteins from the total vesicular fluid of Taenia crassiceps (VF-Tc) were prepared using three different purification methods, consisting of ConA-lectin affinity chromatography (ConA-Tc), preparative electrophoresis (SDS-PAGE) (14 gp-Tc), and monoclonal antibody immunoaffinity chromatography (18/14-Tc). The complex composition represented by the VF-Tc and ConA-Tc antigens revealed peptides ranging from 101- to 14-kDa and from 92- to 12-kDa, respectively. Immunoblotting using lectins confirmed glucose/mannose (glc/man) residues in the 18- and 14-kDa peptides, which are considered specific and immunodominant for the diagnosis of cysticercosis, and indicated that these fractions are glycoproteins. Serum antibodies from a patient with neurocysticercosis that reacted to the 14 gp band from T. crassiceps (Tc) were eluted from immunoblotting membranes and showed reactivity to 14 gp from Taenia solium. In order to determine the similar peptide sequence, the N-terminal amino acid was determined and analyzed with sequences available in public databases. This sequence revealed partial homology between T. crassiceps and T. solium peptides. In addition, mass spectrometry along with theoretical M(r) and pI of the 14 gp-Tc point suggested a close relationship to some peptides of a 150-kDa protein complex of the T. solium previously described. The identification of these common immunogenic sites will contribute to future efforts to develop recombinant antigens and synthetic peptides for immunological assays.
authors.affiliation: Departamento de Patologia, Faculdade de Medicina, Universidade Federal Fluminense, Niterói, Rio de Janeiro, Brazil. peralta@micro.ufrj.br
authors.forename: Regina H
authors.initials: RH
authors.lastname: Peralta
authors.forename: Noeli M
authors.initials: NM
authors.lastname: Espíndola
authors.forename: Alessandra X
authors.initials: AX
authors.lastname: Pardini
authors.forename: Alberto H
authors.initials: AH
authors.lastname: Iha
authors.forename: Hercules
authors.initials: H
authors.lastname: Moura
authors.forename: John R
authors.initials: JR
authors.lastname: Barr
authors.forename: Adelaide J
authors.initials: AJ
authors.lastname: Vaz
authors.forename: José M
authors.initials: JM
authors.lastname: Peralta
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000918:Antibody Specificity; D000947:Antigens, Helminth / Q000737:chemistry* / Q000276:immunology; D015153:Blotting, Western; D002846:Chromatography, Affinity; D003429:Cross Reactions; D003552:Cysticercus / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006023:Glycoproteins / Q000737:chemistry* / Q000276:immunology; D015801:Helminth Proteins / Q000737:chemistry* / Q000276:immunology; D037102:Lectins; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013621:Taenia / Q000276:immunology*; D041201:Taenia solium / Q000276:immunology
chemical_list: D000911:Antibodies, Monoclonal; D000947:Antigens, Helminth; D006023:Glycoproteins; D015801:Helminth Proteins; D037102:Lectins