In silico analysis and developmental expression of ubiquitin-conjugating enzymes in Schistosoma mansoni.

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Data
2015
Autores
Costa, Marcela Pereira
Oliveira, Victor Fernandes de
Pereira, Roberta Verciano
Abreu, Fabiano Carlos Pinto de
Passos, Liana Konovaloff Jannotti
Borges, William de Castro
Cota, Renata Guerra de Sá
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Resumo
Ubiquitin-conjugating enzymes (Ub-E2) perform the second step of ubiquitination and, consequently, are essential for regulating proteolysis and for modulating protein function, interactions and trafficking. Previously, our group demonstrated the crucial role of ubiquitination and the Ubproteasome pathway during the Schistosoma mansoni life cycle. In the present investigation, we used a homology-based genome-wide bioinformatics approach to identify and molecularly characterise the Ub-E2 enzymes in S. mansoni. The putative functions were further investigated through molecular phylogenetic and expression profile analyses using cercariae, adult worms, eggs and mechanically transformed schistosomula (MTS) cultured in vitro for 3.5 h or 1 or 3 days. We identified, via in silico analysis, 17 Ub-E2 enzymes with conserved structural characteristics: the beta-sheet and the helix-2 form a central core bordered by helix-1 at one side and helix-3 and helix-4 at the other. The observed quantitative differences in the steady-state transcript levels between the cercariae and adult worms may contribute to the differential protein ubiquitination observed during the parasite’s life cycle. This study is the first to identify and characterise the E2 ubiquitin conjugation family in S. mansoni and provides fundamental information regarding their molecular phylogenetics and developmental expression during intra-mammalian stages.
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Ubiquitination, Differential expression
Citação
COSTA, M. P. et al. In silico analysis and developmental expression of ubiquitin-conjugating enzymes in Schistosoma mansoni. Parasitology Research, v. 14, n. 5, p. 1769-1777, maio 2015. Disponível em: <https://link.springer.com/article/10.1007%2Fs00436-015-4362-x>. Acesso em: 16 jun. 2017.