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Título: | Characterization of phosphodiesterase-5 as a surface protein in the tegument of Schistosoma mansoni. |
Autor(es): | Rofatto, Henrique Krambeck Tararam, Cibele Aparecida Borges, William de Castro Wilson, R. Alan Leite, Luciana Cesar de Cerqueira Farias, Leonardo Paiva |
Palavras-chave: | Schistosoma mansoni Nucleotide Activity Surface exposed Tegument |
Data do documento: | 2009 |
Referência: | ROFATTO, H. K. et al. Characterization of phosphodiesterase-5 as a surface protein in the tegument of Schistosoma mansoni. Molecular and Biochemical Parasitology, v. 166, p. 32-41, 2009. Disponível em: <https://www.sciencedirect.com/science/article/pii/S0166685109000681>. Acesso em: 08 nov. 2014. |
Resumo: | Schistosoma 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. |
URI: | http://www.repositorio.ufop.br/handle/123456789/4646 |
DOI: | https://doi.org/10.1016/j.molbiopara.2009.02.006 |
ISSN: | 0166-6851 |
Licença: | O periódico Molecular and Biochemical Parasitology concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 3550930939644. |
Aparece nas coleções: | DECBI - Artigos publicados em periódicos |
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Arquivo | Descrição | Tamanho | Formato | |
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ARTIGO_CharacterizationPhosphodiesteraseSurface.pdf | 1,81 MB | Adobe PDF | Visualizar/Abrir |
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