Revista: | Memorias do Instituto Oswaldo Cruz |
Base de datos: | PERIÓDICA |
Número de sistema: | 000349636 |
ISSN: | 0074-0276 |
Autores: | Camacho, Ariane Guglielmi Ariza1 Teixeira, Lais Helena1 Bargieri, Daniel Youssef1 Boscardin, Silvia Beatriz2 Soares, Irene da Silva3 Nussenzweig, Ruth Sonntag4 Nussenzweig, Victor5 Rodrigues, Mauricio Martins1 |
Instituciones: | 1Universidade Federal de Sao Paulo, Escola Paulista de Medicina, Sao Paulo. Brasil 2Universidade de Sao Paulo, Instituto de Ciencias Biomedicas, Sao Paulo. Brasil 3Universidade de Sao Paulo, Faculdade de Ciencias Farmaceuticas, Sao Paulo. Brasil 4University School of Medicine, Michael Heidelberger Division, Nueva York. Estados Unidos de América 5University School of Medicine, Department of Medical and Molecular Parasitology, Nueva York. Estados Unidos de América |
Año: | 2011 |
Volumen: | 106 |
País: | Brasil |
Idioma: | Inglés |
Tipo de documento: | Artículo |
Enfoque: | Experimental, aplicado |
Resumen en inglés | Recently, we described the improved immunogenicity of new malaria vaccine candidates based on the expression of fusion proteins containing immunodominant epitopes of merozoites and Salmonella enterica serovar Typhimurium flagellin (FliC) protein as an innate immune agonist. Here, we tested whether a similar strategy, based on an immunodominant B-cell epitope from malaria sporozoites, could also generate immunogenic fusion polypeptides. A recombinant His6-tagged FliC protein containing the C-terminal repeat regions of the VK210 variant of Plasmodium vivax circumsporozoite (CS) protein was constructed. This recombinant protein was successfully expressed in Escherichia coli as soluble protein and was purified by affinity to Ni-agarose beads followed by ion exchange chromatography. A monoclonal antibody specific for the CS protein of P. vivax sporozoites (VK210) was able to recognise the purified protein. C57BL/6 mice subcutaneously immunised with the recombinant fusion protein in the absence of any conventional adjuvant developed protein-specific systemic antibody responses. However, in mice genetically deficient in expression of TLR5, this immune response was extremely low. These results extend our previous observations concerning the immunogenicity of these recombinant fusion proteins and provide evidence that the main mechanism responsible for this immune activation involves interactions with TLR5, which has not previously been demonstrated for any recombinant FliC fusion protein |
Disciplinas: | Medicina |
Palabras clave: | Parasitología, Inmunología, Paludismo, Flagelina, Proteínas de fusión, Inmunogenicidad, Plasmodium vivax |
Keyword: | Medicine, Parasitology, Immunology, Malaria, Flagellin, Fusion proteins, Immunogenicity, Plasmodium vivax |
Texto completo: | Texto completo (Ver HTML) |