Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 16, Issue 4, Pages S215-S229Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.M116.062448
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Funding
- Wellcome Trust [097997/Z/11/Z, 101602/Z/13/Z, 104914/Z/14/Z]
- BBSRC [BB/N001176/1, BB/K002465/1, BB/I01232X/1]
- National Institutes for Health of the United States of America [AI50237]
- Intramural Research Program of the NIH, NIAID
- Wellcome Trust [101602/Z/13/Z, 097997/Z/11/Z, 104914/Z/14/Z] Funding Source: Wellcome Trust
- BBSRC [BB/K002465/1, BB/I01232X/1, BB/N001176/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/I01232X/1, BB/K002465/1, BB/N001176/1] Funding Source: researchfish
- Medical Research Council [1110704] Funding Source: researchfish
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Noroviruses produce viral RNAs lacking a 5 cap structure and instead use a virus-encoded viral protein genome-linked (VPg) protein covalently linked to viral RNA to interact with translation initiation factors and drive viral protein synthesis. Norovirus infection results in the induction of the innate response leading to interferon stimulated gene (ISG) transcription. However, the translation of the induced ISG mRNAs is suppressed. A SILAC-based mass spectrometry approach was employed to analyze changes to protein abundance in both whole cell and m7GTP-enriched samples to demonstrate that diminished host mRNA translation correlates with changes to the composition of the eukaryotic initiation factor complex. The suppression of host ISG translation correlates with the activity of the viral protease (NS6) and the activation of cellular caspases leading to the establishment of an apoptotic environment. These results indicate that noroviruses exploit the differences between viral VPg-dependent and cellular cap-dependent translation in order to diminish the host response to infection.
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