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  • Review Article
  • Published:

Viral subversion of the host protein synthesis machinery

Nature Reviews Microbiology volume 9, pages 860–875 (2011)Cite this article

Subjects

Key Points

  • Although viruses encode many of the functions that are required for viral replication, they are completely reliant on the protein synthesis machinery that is present in their host cells.

  • Recruiting cellular ribosomes to translate viral mRNAs represents a crucial step in the replication of all viruses.

  • To ensure translation of their mRNAs, viruses use a diverse collection of strategies (probably pirated from their cellular hosts) to commandeer key translation factors that are required for the initiation, elongation and termination steps of translation.

  • Viruses also neutralize host defences that seek to incapacitate the translation machinery in infected cells.

Abstract

Viruses are fully reliant on the translation machinery of their host cells to produce the polypeptides that are essential for viral replication. Consequently, viruses recruit host ribosomes to translate viral mRNAs, typically using virally encoded functions to seize control of cellular translation factors and the host signalling pathways that regulate their activity. This not only ensures that viral proteins will be produced, but also stifles innate host defences that are aimed at inhibiting the capacity of infected cells for protein synthesis. Remarkably, nearly every step of the translation process can be targeted by virally encoded functions. This Review discusses the diverse strategies that viruses use to subvert host protein synthesis functions and regulate mRNA translation in infected cells.

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Figure 1: Overview of mRNA translation in eukaryotes.
The alternative text for this image may have been generated using AI.
Figure 2: Control of cap-dependent translation by regulated assembly of a multisubunit initiation factor.
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Figure 3: Eukaryotic translation initiation factor 2-dependent loading of 40S ribosomes with initiator tRNA regulates translation and is targeted by host antiviral defences.
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Figure 4: Regulation of translation elongation.
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Figure 5: Regulation of translation termination in virus-infected cells.
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Acknowledgements

The authors apologize to the many colleagues whose work is not cited directly here owing to space restrictions. In addition, they thank U. Chuluunbaatar and L. Shiflett for critical reading of the manuscript. Grants from the US National Institutes of Health (I.M.), Science Foundation Ireland (D.W.) and the Irish Health Research Board (D.W.) funded research in the authors' laboratories.

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  1. Derek Walsh

    Present address: Present address: Department of Microbiology, New York University School of Medicine, New York, New York 10016, USA.,

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  1. National Institute for Cellular Biotechnology, Dublin City University, 9, Dublin, Ireland

    Derek Walsh

  2. Department of Microbiology and New York University Cancer Institute, New York University School of Medicine, New York, 10016, New York, USA

    Ian Mohr

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Glossary

7-methylguanosine cap

A 7-methylguanosine linked to the 5′ end of an mRNA, via a 5′–5′ triphosphate linkage, to mark the extreme 5′ terminus of a eukaryotic mRNA. In addition to having regulatory roles in pre-mRNA processing and mRNA stability, the cap structure controls ribosome recruitment to the mRNA 5′ end.

Internal ribosome entry sites

(IRESs). Cis-acting structural elements that lie within mRNAs and mediate cap-independent ribosome recruitment. Different IRES elements have varying requirements for translation initiation factors.

IRES-transactivating factors

(ITAFs). Trans-acting protein cofactors that are required by some internal ribosome entry sites (IRESs), in addition to canonical translation initiation factors, in order to promote IRES-dependent translation initiation.

Polycistronic

Of an mRNA: containing multiple ORFs or cistrons. In eukaryotes, most mRNAs are monocistronic, and specific cis-acting elements are required to efficiently translate polycistronic mRNAs. Polycistronic mRNAs, however, are relatively common in bacteria and archaea.

Autophagy

A catabolic process whereby cytoplasmic components (proteins or organelles) are targeted to lysosomes for recycling, providing the nutrients that are required during starvation, growth factor withdrawal, infection or oxidative stress.

Pseudosubstrates

Proteins that resemble a natural substrate sufficiently that they bind the target enzyme and subsequently inhibit recognition of the natural substrate by acting as decoys. The enzyme typically does not modify the pseudosubstrate. For example, virally encoded PKR pseudosubstrates are not phosphorylated by PKR, but they effectively bind PKR and prevent phosphorylation of eukaryotic translation initiation factor 2α, the natural PKR substrate.

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Walsh, D., Mohr, I. Viral subversion of the host protein synthesis machinery. Nat Rev Microbiol 9, 860–875 (2011). https://doi.org/10.1038/nrmicro2655

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