Foot-and-Mouth Disease Virus Leader Proteinase
Key result
Self-processing of the foot-and-mouth disease virus leader proteinase requires a basic residue at one side of the scissile bond and acts as an intramolecular reaction.
Population
Rabbit reticulocyte lysate system examining foot-and-mouth disease virus leader proteinase (L(pro))
Comparison
Mutations/substitutions in the cleavage site and… vs Wild-type L(pro)
Design
Preclinical
Authors
Discussion
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Member takes
Implication
No immediate clinical implications; leaves open targeted antiviral strategies pending mammalian validation.
Structured PICO
P
Population
Rabbit reticulocyte lysate system examining foot-and-mouth disease virus leader proteinase (L(pro))
I
Intervention
Mutations/substitutions in the cleavage site (leucine and lysine to serine and glutamine) and removal/replacement of the 18-amino acid C-terminal extension of L(pro)
C
Comparator
Wild-type L(pro)
O
Outcome
Rate and efficiency of self-processing and eIF4GI cleavagesurrogate
The study demonstrates that self-processing of the foot-and-mouth disease virus leader proteinase is an intramolecular reaction requiring a basic residue at the scissile bond.
Cite This Study
Glaser et al. (2001) studied Foot-and-mouth disease virus. L(pro) mutations/variants vs. wild-type L(pro) was evaluated on Substrate specificity and cleavage reactions of L(pro). Self-processing of the foot-and-mouth disease virus leader proteinase requires a basic residue at one side of the scissile bond and acts as an intramolecular reaction.