Purification and partial characterization of coxsackievirus B3 2A protease expressed in Escherichia coli

Abstract

Reported here is the overexpression, purification and partial characterization of recombinant coxsakievirus B3 2A protease (CVB3 2Apro) from bacterial cells transformed with a plasmid containing the CVB3 2Apro cDNA sequences. The structural investigation showed that the protein contains mostly beta-strand elements and requires Zn2+ ions as a structural component which appeared to be inhibitory if added exogenously. The purified enzyme activity was optimal at 4 degrees C and had a short half-life at physiological temperature. This feature can be the result of the presence of a high content of beta-structure and also hydrophobic residues in its structure.