Journal article
Identification of critical amino acids within the foot-and-mouth disease virus leader protein, a cysteine protease
The Leader protein of foot-and-mouth disease virus (FMDV) is the first component of the virus polyprotein. It is synthesized in two forms, Lab and Lb, both of which display the ability to cleave the L/P1 junction in trans and to induce the cleavage of the cap-binding complex component eIF-4G (p220).
The L protease has weak homology to the family of cysteine proteases, which have a catalytic dyad composed of a cysteine and a histidine. Mutations have been introduced into FMDV cDNA to modify each of the four cysteine residues and the three conserved histidine residues within the Lb species. The activities of the mutant L proteins have been determined.
Modification of a single cysteine residue (residue 51) or of a single histidine residue (residue 148) abolished the abilities of L to cleave the L/P1 junction and to inhibit cap-dependent protein synthesis. In contrast, modification of each of the other cysteine residues and other conserved histidine residues had no apparent effect on these activities.
Language: | English |
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Publisher: | Elsevier BV |
Year: | 1995 |
Pages: | 140-146 |
ISSN: | 1089862x , 00426822 and 10960341 |
Types: | Journal article |
DOI: | 10.1006/viro.1995.1554 |
ORCIDs: | Belsham, G J |
Amino Acid Sequence Amino Acids Animals Aphthovirus Base Sequence Cysteine Cysteine Endopeptidases DNA Primers DNA, Viral Endopeptidases Guinea Pigs Histidine Humans Molecular Sequence Data Mutagenesis, Site-Directed Plasmids Protein Sorting Signals Sequence Alignment Sequence Homology, Amino Acid leader proteinase, foot-and-mouth disease virus