Cleavage of eukaryotic initiation factor eIF4G and inhibition of host-cell protein synthesis during feline calicivirus infection
Autor: | Michael J. Carter, Lisa O. Roberts, Margaret M. Willcocks |
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Rok vydání: | 2004 |
Předmět: |
viruses
Cell Line chemistry.chemical_compound Eukaryotic translation Virology Eukaryotic initiation factor Protein biosynthesis Animals Initiation factor Caliciviridae Infections mRNA Cleavage and Polyadenylation Factors Feline calicivirus biology EIF4G Calicivirus Proteins virus diseases biochemical phenomena metabolism and nutrition biology.organism_classification Caliciviridae chemistry Protein Biosynthesis Cats Eukaryotic Initiation Factor-4G Calicivirus Feline |
Zdroj: | Journal of General Virology. 85:1125-1130 |
ISSN: | 1465-2099 0022-1317 |
DOI: | 10.1099/vir.0.19564-0 |
Popis: | Caliciviruses are small, non-enveloped, positive-stranded RNA viruses that are pathogenic for both animals and man. Although their capsid structure and genomic organization are distinct from picornaviruses, they have similarities to these viruses in their non-structural proteins. Picornaviruses induce a rapid inhibition of host-cell cap-dependent protein synthesis and this is mainly achieved through cleavage of eIF4G and/or dephosphorylation of 4E-BP1. In this study, the effect of calicivirus infection was examined on host-cell protein synthesis in order to determine whether they also induce host shut-off. We report that infection of cells with feline calicivirus (FCV) leads to the inhibition of cellular protein synthesis. This is accompanied by the cleavage of the eukaryotic translation initiation factors eIF4GI and eIF4GII in a manner reminiscent of that induced by picornaviruses. However, the cleavages occur at different sites. The potential mechanisms of these cleavage events and the implications for the translation of calicivirus mRNA are discussed. |
Databáze: | OpenAIRE |
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