What does this research mean for the field?

The C-terminal 19 amino acids of cardiovirus 2A proteins are sufficient to mediate high-efficiency polyprotein cleavage, comparable to the short aphthovirus 2A protein, whose activity is further enhanced by upstream viral sequences. Novelty: ClaimNovelty.INCREMENTAL. Consensus alignment: ConsensusAlignment.NEUTRAL.

January 1, 1997Journal of General Virology

The cleavage activities of aphthovirus and cardiovirus 2A proteins.

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Population

Artificial polyprotein systems (CAT-2A-GUS) and prokaryotic translation systems

Design

Preclinical

Authors

MDMichelle DonnellyUniversity of Massachusetts Lowell MRMartin D. RyanUniversity of St Andrews MFMike FlintCenters for Disease Control and Prevention

Discussion

Member takes

Implication

May aid recombinant polyprotein engineering; leaves open translation beyond in vitro models.

Structured PICO

Population

Artificial polyprotein systems (CAT-2A-GUS) and prokaryotic translation systems

Intervention

Insertion of FMDV capsid protein 1 D sequences, TME 2A protein, or EMC 2A protein sequences

Outcome

Cleavage efficiencysurrogate

The study demonstrates that specific sequences from aphthovirus and cardiovirus 2A proteins can mediate high-efficiency cleavage in artificial polyprotein systems.

Cite This Study

Donnelly et al. (1997) studied this question.

synapsesocial.com/papers/6a1e69c5fe0256fbba3296bb https://doi.org/10.1099/0022-1317-78-1-13

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The cleavage activities of aphthovirus and cardiovirus 2A proteins.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

The cleavage activities of aphthovirus and cardiovirus 2A proteins.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider