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Title: The Trypanosoma cruzi virulence factor Oligopeptidase B (OPBTc) assembles into an active and stable dimer
Authors: Motta, Flávia da Silva Nader
Bastos, Izabela Marques Dourado
Faudry, Eric
Ebel, Christine
Lima, Meire Maria de
Neves, David
Ragno, Michel
Barbosa, João Alexandre R G
Freitas, Sônia Maria de
Santana, Jaime Martins de
Assunto:: Tripanossoma cruzi
Chagas, Doença de
Issue Date: Jan-2012
Publisher: Plos UM
Citation: MOTTA, Flávia da Silva Nader et al. The Trypanosoma cruzi virulence factor Oligopeptidase B (OPBTc) assembles into an active and stable dimer. Plos One, v. 7, n. 1, jan. 2012. Disponível em: <>. Acesso em: 18 dez. 2012.
Abstract: Oligopeptidase B, a processing enzyme of the prolyl oligopeptidase family, is considered as an important virulence factor intrypanosomiasis. Trypanosoma cruzi oligopeptidase B (OPBTc) is involved in host cell invasion by generating a Ca2+-agonist necessary for recruitment and fusion of host lysosomes at the site of parasite attachment. The underlying mechanism remains unknown and further structural and functional characterization of OPBTc may help clarify its physiological function and lead to the development of new therapeutic molecules to treat Chagas disease. In the present work, size exclusion chromatography and analytical ultracentrifugation experiments demonstrate that OPBTc is a dimer in solution, an association salt and pH-resistant and independent of intermolecular disulfide bonds. The enzyme retains its dimeric structure and is fully active up to 42uC. OPBTc is inactivated and its tertiary, but not secondary, structure is disrupted at higher temperatures, as monitored by circular dichroism and fluorescence spectroscopy. It has a highly stable secondary structure over a broad range of pH, undergoes subtle tertiary structure changes at low pH and is less stable under moderate ionic strength conditions. These results bring new insights into the structural properties of OPBTc, contributing to future studies on the rational design of OPBTc inhibitors as a promising strategy for Chagas disease chemotherapy.
Licença:: Todo o conteúdo deste periódico, exceto onde está identificado, está licenciado sob uma Licença Creative Commons (Attribution 2.5 Generic (CC BY 2.5)). Fonte: Acesso em: 18 dez. 2012.
Appears in Collections:CEL - Artigos publicados em periódicos

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