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Type: Artigo de Periódico
Title: Immunostimulatory property of a synthetic peptide belonging to the soluble ATP diphosphohydro-lase isoform (SmATPDase 2) and immunolocalisation of this protein in the Schistosoma mansoni egg
Author: Mendes, Rita Gabriela Pedrosa Ribeiro
Gusmão, Michélia Antônia do Nascimento
Maia, Ana Carolina Ribeiro Gomes
Detoni, Michelle de Lima
Porcino, Gabriane Nascimento
Soares, Thais Vieira
Juliano, Maria Aparecida
Juliano, Luiz
Coelho, Paulo Marcos Zech
Lenzi, Henrique Leonel
Pinto, Priscila Faria
Vasconcelos, Eveline Gomes
Resumo: -
Abstract: A peptide (SmB2LJ; r175-194) that belongs to a conserved domain from Schistosoma mansoni SmATPDase 2 and is shared with potato apyrase, as predicted by in silico analysis as antigenic, was synthesised and its immunostimulatory property was analysed. When inoculated in BALB/c mice, this peptide induced high levels of SmB2LJ-specific IgG1 and IgG2a subtypes, as detected by enzyme linked immunosorbent assay. In addition, dot blots were found to be positive for immune sera against potato apyrase and SmB2LJ. These results suggest that the conserved domain r175-194 from the S. mansoni SmATPDase 2 is antigenic. Western blots were performed and the anti-SmB2LJ antibody recognised in adult worm (soluble worm antigen preparation) or soluble egg antigen antigenic preparations two bands of approximately 63 and 55 kDa, molecular masses similar to those predicted for adult worm SmATPDase 2. This finding strongly suggests the expression of this same isoform in S. mansoni eggs. To assess localisation of SmATPDase 2, confocal fluorescence microscopy was performed using cryostat sections of infected mouse liver and polyclonal antiserum against SmB2LJ. Positive reactions were identified on the external surface from the miracidium in von Lichtenberg's envelope and, in the outer side of the egg-shell, showing that this soluble isoform is secreted from the S. mansoni eggs.
Keywords: Schistosoma mansoni
Potato apyrase
CNPq: -
Language: eng
Country: Brasil
Publisher: -
Institution Initials: -
Access Type: Acesso Aberto
Issue Date: 2011
Appears in Collections:Artigos de Periódicos

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