Taenia crassiceps cysticerci: Characterization of the 14-kDa glycoprotein with homologies to antigens from Taenia solium cysticerci

Autor(es)

Peralta, Regina H. ^[1] ; Espindola, Noeli M. ^[2] ; Pardini, Alessandra X. ^[2] ; Iha, Alberto H. ^[2] ; Moura, Hercules ^[3] ; Barr, John R. ^[3] ; Vaz, Adelaide J. ^[2] ; Peralta, Jose M. ^[4]

Afiliação do(s) autor(es)

^[1] Univ Fed Fluminense, Fac Med, Dept Patol, Rio De Janeiro - Brazil

^[2] Univ Sao Paulo, Fac Ciencias Farmaceut, Lab Imunol Clin, Sao Paulo - Brazil

^[3] Ctr Dis Control & Prevent, Natl Ctr Environm Hlth, Atlanta, GA - USA

^[4] Univ Fed Rio de Janeiro, Inst Microbiol, Dept Imunol, BR-21941590 Rio De Janeiro - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Experimental Parasitology; v. 124, n. 3, p. 295-300, MAR 2010.
• Citações Web of Science: 8

Resumo

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) (14gp-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 14gp band from T. crassiceps (Tc) were eluted from immunoblotting membranes and showed reactivity to 14gp 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 14gp-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. (C) 2009 Elsevier Inc. All rights reserved. (AU)

• Processo FAPESP: 02/12061-0 - Cisticercose: imunodiagnóstico, antígenos, resposta imunológica e aspectos clínico-epidemiológicos
• Beneficiário: Adelaide José Vaz
• Linha de fomento: Auxílio à Pesquisa - Temático