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. 2020 Oct 9;11:565142. doi: 10.3389/fimmu.2020.565142

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Copyright © 2020 Cerny, Bivona, Sanchez Alberti, Trinitario, Morales, Cardoso Landaburu, Cazorla and Malchiodi.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Cloning and characterization of Chg. (A) Digestion of pET23a⁺-Chg construction with the NdeI and HindIII restriction enzymes released the 400-bp Chg insert. (B) SDS-PAGE analysis of rChg expression in E. coli BL21 and purification under native condition. Lane 1: MW marker; Lane 2: IMAC Ni-NTA purified rChg (12 kDa) stained with Coomassie Brilliant Blue. (C) Relative enzymatic activity of T. cruzi epimastigote lysate (5 μM) in the presence of rChg (10 μM) or synthetic inhibitor E-64 (10 μM) on the fluorogenic substrate Z-Gly-Pro-AMC (6 μg) measured as relative fluorescent units (RFUs) and expressed as the log of the percentage of the fluorescence units as a function of time. (D) Cysteine protease activity of the rNtCz in the absence or presence of increasing concentrations of rChg (0.01–10 μg).