Cleavage of foot-and-mouth disease virus polyprotein is mediated by residues located within a 19 amino acid sequence

• Published in: Journal of general virology 1991-11, Vol.72 (11), p.2727-2732
• Main Authors: Ryan, Martin D, King, Andrew M. Q, Thomas, G. Paul
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Aphthovirus - metabolism; Base Sequence; Biological and medical sciences; Cell-Free System; DNA, Viral; Endopeptidases - metabolism; foot-and-mouth disease virus; Fundamental and applied biological sciences. Psychology; Microbiology; Molecular Sequence Data; Plasmids; Protein Biosynthesis; Protein Processing, Post-Translational; Proteins - metabolism; Rabbits; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains; Restriction Mapping; Viral Proteins - metabolism; Virology
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-72-11-2727

AFRC Institute for Animal Health, Pirbright Laboratory, Ash Road, Pirbright, Woking, Surrey GU24 0NF, U.K. The 2A region of the foot-and-mouth disease virus (FMDV) polyprotein is only 16 amino acids in length. During synthesis of the FMDV polyprotein a primary proteolytic processing event occurs between the 2A and 2B regions of the polyprotein. The activity responsible for this cleavage is not known but it is thought that either an unidentified virus-encoded proteinase may be responsible, or that 2A acts as a substrate for a host cell proteinase. A series of recombinant FMDV polyproteins has been constructed in which sequences to the N- or C-terminal side of the 2A region have been deleted. Analysis of the processing of these polyproteins shows that a 19 amino acid sequence spanning 2A is sufficient to mediate polyprotein cleavage at a site immediately C-terminal to 2A, whereas deletions extending into the 2A region prevent cleavage. Received 8 May 1991; accepted 25 July 1991.