Key result
A mutant poliovirus precursor with a single amino acid insertion near the carboxy-terminal Q-G site can cleave at the amino-terminal site but cannot undergo self-cleavage at the carboxy-terminal site.
Population
Bacterial expression system transformed with recombinant plasmid containing poliovirus genome cDNA region…
Comparison
Site-specific mutagenesis vs Wild-type construct (pIN-III-C3-7c)
Design
Preclinical
Authors
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Site-specific cleavage defects in poliovirus precursor; leaves open avenues for disrupting polyprotein processing in antiviral research.
Site-specific mutagenesis of poliovirus proteinase 3C demonstrates that a single amino acid insertion near the carboxy-terminal cleavage site abolishes self-cleavage at that site while preserving amino-terminal cleavage activity.
Semler et al. (1987) studied this question. Site-specific mutagenesis (single amino acid insertion near carboxy-terminal Q-G cleavage site) vs. Wild-type construct (pIN-III-C3-7c) was evaluated on Autocatalytic cleavage of proteinase 3C. A mutant poliovirus precursor with a single amino acid insertion near the carboxy-terminal Q-G site can cleave at the amino-terminal site but cannot undergo self-cleavage at the carboxy-terminal site.
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