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

• Autor(a) principal: Rofatto, Henrique Krambeck
• Data de Publicação: 2009
• Outros Autores: Tararam, Cibele Aparecida, Borges, William de Castro, Wilson, R. Alan, Leite, Luciana Cesar de Cerqueira, Farias, Leonardo Paiva
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UFOP
• Texto Completo: http://www.repositorio.ufop.br/handle/123456789/4646; https://doi.org/10.1016/j.molbiopara.2009.02.006
• topic: Schistosoma mansoni; Nucleotide; Activity; Surface exposed; Tegument

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.