Key result
In vitro proteolysis experiments indicated that all seven cleavage-defective mutants of encephalomyocarditis virus have capsid precursors with a temperature-sensitive configuration.
Population
Encephalomyocarditis virus (wild-type and seven temperature-sensitive capsid cleavage mutants)
Comparison
In vitro proteolysis reactions at 38 degrees C vs Wild-type viral RNA and capsid precursors
Design
Preclinical
Authors
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No immediate clinical implications for EMCV myocarditis; leaves open in vivo validation of precursor configuration in viral maturation.
The study demonstrates that the cleavage defect in temperature-sensitive mutants of encephalomyocarditis virus is due to a temperature-sensitive configuration of the capsid precursors rather than the viral protease.
Young et al. (1982) studied Encephalomyocarditis virus. Temperature-sensitive capsid cleavage mutants vs. Wild-type encephalomyocarditis virus was evaluated on In vitro proteolysis of capsid precursors at 38 degrees C. In vitro proteolysis experiments indicated that all seven cleavage-defective mutants of encephalomyocarditis virus have capsid precursors with a temperature-sensitive configuration.
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