We investigated the possible translational role which elevated concentrations of highly purified Semliki Forest virus (SFV) capsid (C)-protein molecules may play in a cell-free translation system. Here we decomonstrate that in the absence of double-stranded RNA high concentrations of C protein triggered the phosphorylation of the interferon-induced, double-stranded RNA-activated protein kinase, PKR. Activated PKR in turn phosphorylated its natural substrate, the α subunit of eukaryotic initiation factor 2 (eIF-2), thereby inhibiting initiation of host cell translation. These findings were further strengthened by experiments showing that during natural infection with SFV the maximum phosphorylation of PKR coincided with the maximum synthesis of C protein 4–9 hours post infection. Thus, our results demonstrate that high concentrations of C-protein molecules may act in a hitherto novel mechanism on PKR to inhibit host cell protein synthesis during viral infection.
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Research Article|
December 01 1996
Semliki forest virus capsid protein inhibits the initiation of translation by upregulating the double-stranded RNA-activated protein kinase (PKR)
Daniel Favre;
Daniel Favre
1Institute of Medical Microbiology, University of Berne, Friedbühlstrasse 51, CH-3010 Berne, Switzerland.
2Department of Biochemistry and McGill Cancer Center, McGill University, Montreal, Canada.
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Erwin Studer;
Erwin Studer
1Institute of Medical Microbiology, University of Berne, Friedbühlstrasse 51, CH-3010 Berne, Switzerland.
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Marcel R. Michel
Marcel R. Michel
1Institute of Medical Microbiology, University of Berne, Friedbühlstrasse 51, CH-3010 Berne, Switzerland.
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Publisher: Portland Press Ltd
Received:
October 07 1996
Accepted:
November 05 1996
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1996 Plenum Publishing Corporation
1996
Biosci Rep (1996) 16 (6): 485–511.
Article history
Received:
October 07 1996
Accepted:
November 05 1996
Citation
Daniel Favre, Erwin Studer, Marcel R. Michel; Semliki forest virus capsid protein inhibits the initiation of translation by upregulating the double-stranded RNA-activated protein kinase (PKR). Biosci Rep 1 December 1996; 16 (6): 485–511. doi: https://doi.org/10.1007/BF01198464
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