PMID:9010280

Citation	Donnelly, ML, Gani, D, Flint, M, Monaghan, S and Ryan, MD (1997) The cleavage activities of aphthovirus and cardiovirus 2A proteins. J. Gen. Virol. 78 ( Pt 1):13-21
Abstract	The primary 2A/2B polyprotein cleavage of aphtho-and cardioviruses is mediated by their 2A proteins cleaving C-terminally. Whilst the aphthovirus 2A region is only 16 aa (possibly 18 aa) long, the cardiovirus 2A protein is some 150 aa. We have previously shown that foot-and-mouth disease virus (FMDV) 2A is able to mediate cleavage in an artificial (chloramphenicol acetyltransferase/FMDV 2A/beta-glucuronidase [CAT-2A-GUS]) polyprotein system devoid of any other FMDV sequences with high (approximately 85%), although not complete, cleavage. In this paper we show that insertion of upstream FMDV capsid protein 1 D sequences increases the activity. In addition, we have demonstrated that the cardiovirus Theiler's murine encephalomyelitis virus(TME) 2A protein, when linked to GUS in a single ORF, is able to cleave at its own C terminus with high efficiency--if not completely. The C-terminal 19 aa of TME 2A, together with the N-terminal proline residue of protein 2B, were inserted into the CAT/GUS artificial polyprotein system (in a single ORF). This recombinant [CAT-deltaTME2A-GUS] polyprotein was able to mediate cleavage with high (approximately 85%) efficiency--directly comparable to the activity observed when FMDV 2A was inserted. A similar insertion into [CAT-GUS] of the C-terminal 19 aa of the cardiovirus encephalomyocarditis virus (EMC) 2A, together with the N-terminal proline residue of protein 2B, produced a [CAT-delta EMC2A-GUS] polyprotein which also mediated cleavage at approximately 85%. Analysis of the products of expression of these artificial polyproteins in a prokaryotic translation system did not, apparently, reveal any GUS cleavage product.
Links	PubMed
Keywords	Amino Acid Sequence; Animals; Aphthovirus/metabolism; Base Sequence; Cardiovirus/metabolism; Chloramphenicol O-Acetyltransferase/biosynthesis; DNA Primers; Molecular Sequence Data; Plasmids; Polymerase Chain Reaction; Protein Biosynthesis; Rabbits; Recombinant Fusion Proteins/biosynthesis; Reticulocytes/metabolism; Sequence Homology, Amino Acid; Transcription, Genetic; Viral Proteins/biosynthesis; Viral Proteins/chemistry; Viral Proteins/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
TMEVG:POLG		GO:0097264: self proteolysis	ECO:0000314:		P		Figure 4.	complete CACAO 10478

References

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