Key result
The murine coronavirus MHV-A59 expresses an active 3C-like proteinase that utilizes at least one canonical QS dipeptide as a cleavage site in vitro.
Population
In vitro transcription-translation system expressing a cDNA fragment containing the putative 3C-like…
Comparison
Mutations at the putative catalytic histidine… vs Wild-type construct (pGpro)
Design
Preclinical
Authors
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May guide conserved coronavirus proteinase targeting; leaves open validation in human cells and disease models.
This study confirms that coronaviruses express an active proteinase within the 3C-like proteinase domain of gene 1 ORF 1a that utilizes a canonical QS dipeptide as a cleavage site.
Lü et al. (1995) studied Murine coronavirus MHV-A59. cDNA fragment containing the putative 3C-like proteinase domain of MHV-A59 vs. Mutations at the putative catalytic histidine and cysteine residues was evaluated on Cleavage of the 27-kDa protein. The murine coronavirus MHV-A59 expresses an active 3C-like proteinase that utilizes at least one canonical QS dipeptide as a cleavage site in vitro.
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