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Home / Publications / Expression and characterization of the Babesia bigemina cysteine protease BbiCPL1.

Expression and characterization of the Babesia bigemina cysteine protease BbiCPL1.

  • Authors: Martins TM, Do Rosário VE, Domingos A
  • Journal: Acta Tropica
  • Link: http://www.ncbi.nlm.nih.gov/pubmed/?term=Expression+and+characterization+of+the+Babesia+bigemina+cysteine+protease+babesipain-1.

BbiCPL1 was the first papain-like cysteine protease from a piroplasm to be identified with proteolytic activity. Here we report the improved production of the active recombinant enzyme, and the biochemical characterization of this potential drug target. BbiCPL1 showed characteristic properties of its class, including hydrolysis of papain-family peptide substrates, an acidic pH optimum, requirement of a reducing environment for maximum activity, and inhibition by standard cysteine protease inhibitors such as E-64, leupeptin, ALLN and cystatin. The optimum pH for the protease activity against peptide substrates was 5.5, but enzymatic activity was observed between pH 4.0 and pH 9.0. At slightly basic pH 7.5, BbiCPL1 maintained 83% of maximum activity, suggesting a role in cytosol environment.

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About GHTM

GHTM is a R&D Unit that brings together researchers with a track record in Tropical Medicine and International & Global Health. It aims at strengthening Portugal's role as a leading partner in the development and implementation of a global health research agenda. Our evidence-based interventions contribute to the promotion of equity in health and to improve the health of populations.

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