Identification of critical amino acids within the foot-and-mouth disease virus Leader protein, a cysteine protease
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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.
Originalsprog | Engelsk |
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Artikelnummer | 71554 |
Tidsskrift | Virology |
Vol/bind | 213 |
Udgave nummer | 1 |
Sider (fra-til) | 140-146 |
Antal sider | 7 |
ISSN | 0042-6822 |
DOI | |
Status | Udgivet - 20 okt. 1995 |
ID: 379029435