Key result
Recombinant poliovirus 3C protease expressed in E. coli successfully cleaved the Gln-Gly peptide bond in virus polyprotein, beta-galactosidase, and bovine catalase.
Recombinant poliovirus 3C protease retains specific proteolytic activity and can cleave specific peptide bonds in various proteins.
No immediate clinical implications; leaves open protease engineering tools for future mechanistic studies.
Active 3C protease of poliovirus 1(M) was obtained when cloning and expressing fragment HindII-HindIII (bases from 5240 to 6056) of cDNA in vector pTTQ8 in E.coli cells. As shown, fragment 3D of polymerase covalently bound to 3C does not deprive the enzyme of its specific proteolytic activity. The absence of 26 N-terminal amino acids in 3C entails its inactivation. The recombinant 3C protease cleaved peptide bond Gln-Gly not only in virus polyprotein, but also in molecules of beta-galactosidase and bovine catalase.
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Sablina et al. (1991) studied this question. Recombinant poliovirus 3C protease was evaluated on Proteolytic activity (cleavage of peptide bond Gln-Gly). Recombinant poliovirus 3C protease expressed in E. coli successfully cleaved the Gln-Gly peptide bond in virus polyprotein, beta-galactosidase, and bovine catalase.
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