Antiviral effects of a thiol protease inhibitor on foot-and-mouth disease virus

The thiol protease inhibitor E-64 specifically blocks autocatalytic activity of the leader protease of foot-and-mouth disease virus (FMDV) and interferes with cleavage of the structural protein precursor in an in vitro translation assay programmed with virion RNA. Experiments with FMDV-infected cell...

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Published inJournal of Virology Vol. 66; no. 12; pp. 7168 - 7175
Main Authors Kleina, L.G. (Plum Island Animal Disease Center, ARS, USDA, Greenport, NY), Grubman, M.J
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.12.1992
Subjects
Animals
Antibiotics. Antiinfectious agents. Antiparasitic agents
ANTIMETABOLITE
ANTIMETABOLITOS
ANTIVIRAL
Antiviral agents
Antiviral Agents - pharmacology
Aphthovirus - drug effects
Aphthovirus - physiology
Biological and medical sciences
Cattle
Cell Line
foot-and-mouth disease virus
INHIBIDORES DE ENZIMAS
INHIBITEUR D'ENZYME
Kidney
Kinetics
Medical sciences
Pharmacology. Drug treatments
PROTEASAS
PROTEASE
Protease Inhibitors - pharmacology
Protein Precursors - metabolism
Protein Processing, Post-Translational - drug effects
Viral Structural Proteins - biosynthesis
VIRICIDAS
VIRUS FIEBRE AFTOSA
VIRUS FIEVRE APHTEUSE
Virus Replication - drug effects
Virus
Morphogenesis
Aphthovirus
Enzyme
Picornaviridae
Protein synthesis
Cysteine proteinase
Enzyme inhibitor
Antiviral
Inhibition
In vitro
Biological activity
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Summary:The thiol protease inhibitor E-64 specifically blocks autocatalytic activity of the leader protease of foot-and-mouth disease virus (FMDV) and interferes with cleavage of the structural protein precursor in an in vitro translation assay programmed with virion RNA. Experiments with FMDV-infected cells and E-64 or a membrane-permeable analog, E-64d, have confirmed these results and demonstrated interference in virus assembly, causing a reduction in virus yield. In addition, there is a lag in the appearance of virus-induced cellular morphologic alterations, a delay in cleavage of host cell protein p220 and in shutoff of host protein synthesis, and a decrease in viral protein and RNA synthesis. The implications of using E-64-based compounds as potential antiviral agents for FMDV are discussed
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ISSN:0022-538X
1098-5514
DOI:10.1128/JVI.66.12.7168-7175.1992