Characterization of phosphodiesterase-5 as a surface protein in the tegument of Schistosoma mansoni.

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MetadadosDescriçãoIdioma
Autor(es): dc.creatorRofatto, Henrique Krambeck-
Autor(es): dc.creatorTararam, Cibele Aparecida-
Autor(es): dc.creatorBorges, William de Castro-
Autor(es): dc.creatorWilson, R. Alan-
Autor(es): dc.creatorLeite, Luciana Cesar de Cerqueira-
Autor(es): dc.creatorFarias, Leonardo Paiva-
Data de aceite: dc.date.accessioned2019-11-06T13:32:46Z-
Data de disponibilização: dc.date.available2019-11-06T13:32:46Z-
Data de envio: dc.date.issued2015-03-16-
Data de envio: dc.date.issued2015-03-16-
Data de envio: dc.date.issued2009-
Fonte completa do material: dc.identifierhttp://www.repositorio.ufop.br/handle/123456789/4646-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/557728-
Descrição: dc.descriptionSchistosoma mansoni is a major causative agent of schistosomiasis, an important parasitic disease that constitutes a severe health problem in developing countries. Even though an effective treatment exists, it does not prevent re-infection and the development of an effective vaccine still remains the most desirable means of control for this disease. In thisworkwe describe the cloning and characterization of a S. mansoni nucleotidepyrophosphatase/phosphosdiesterase type 5(SmNPP-5), previously identifiedinthe tegument by proteomic studies. In silico analysis predicts an N-terminal signal peptide, three N-glycosylation sites and a C-terminal transmembrane domain similar to that described for mammalian isoforms. Real-time quantitative RT-PCR andWestern blot analyses determined that SmNPP-5 is significantly upregulated in the transition from free-living cercaria to schistosomulum and adult worm parasitic stages; additionally, the native protein was demonstrated to be N-glycosylated. Immunolocalization experiments and tegument surface membrane preparations confirm the protein as a tegument surface protein. Furthermore, the ectolocalization of this enzyme was corroborated through the hydrolysis of the phosphodiesterase specific substrate (_-Nph-5_-TMP) by living adult and 21-day-old worms. Interestingly, pre-incubation of adult and 21-day-old worms with anti-rSmNPP-5 antibody was able to reduce by 50–60% the enzyme activity. These results suggest that SmNPP-5 is closely associated with the new tegument surface generation after cercarial penetration, and being located at the host–parasite interface, is a potential target for immune intervention.-
Idioma: dc.languageen-
Direitos: dc.rightsO Periódico Molecular and Biochemical Parasitology concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 3550930939644.-
Palavras-chave: dc.subjectSchistosoma mansoni-
Palavras-chave: dc.subjectNucleotide-
Palavras-chave: dc.subjectActivity-
Palavras-chave: dc.subjectSurface exposed-
Palavras-chave: dc.subjectTegument-
Título: dc.titleCharacterization of phosphodiesterase-5 as a surface protein in the tegument of Schistosoma mansoni.-
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