Norovirus Translation Requires an Interaction between the C Terminus of the Genome-linked Viral Protein VPg and Eukaryotic Translation Initiation Factor 4G

Chung, Liliane; Bailey, Dalan; Leen, Eoin N; Emmott, Edward; Chaudhry, Yasmin; Roberts, Lisa O.; Curry, Stephen; Locker, Nicolas; Goodfellow, Ian

doi:10.1074/jbc.m114.550657

Cited by 53 publications

(100 citation statements)

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“…Most of the proteins identified were components of the host cell translation 91 complex including ribosomal proteins, translation initiation factors and host RNA 92 binding proteins. These data agrees with but significantly extend our previous 93 observations using a less sensitive multi-step affinity purification approach to 94 characterise host factors associated with the MNV VPg protein only (Chaudhry et al, 95 2006;Chung et al, 2014). In addition, we identified hnRNPA1 which we have 96 previously shown to act in norovirus genome circularization (López-Manríquez et al, 97 2013).…”

supporting

confidence: 84%

Noroviruses subvert the core stress granule component G3BP1 to promote viral VPg-dependent translation

Hosmillo

Jia

McAllaster

et al. 2019

Preprint

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148) 1Knowledge of the host factors required for norovirus replication has been hindered 2 by the challenges associated with culturing human noroviruses. We have combined 3 proteomic analysis of the viral translation and replication complexes with a CRISPR 4 screen, to identify host factors required for norovirus infection. The core stress 5 granule component G3BP1 was identified as a host factor essential for efficient 6 human and murine norovirus infection, demonstrating a conserved function across 7 the Norovirus genus. Furthermore, we show that G3BP1 functions in the novel 8 paradigm of viral VPg-dependent translation initiation, contributing to the assembly of 9 translation complexes on the VPg-linked viral positive sense RNA genome by 10 facilitating 40S recruitment. Our data suggest that G3BP1 functions by providing viral 11 RNA a competitive advantage over capped cellular RNAs, uncovering a novel 12 function for G3BP1 in the life cycle of positive sense RNA viruses and identifying the 13 first host factor with pan-norovirus pro-viral activity. 14 15 16

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supporting

confidence: 84%

Noroviruses subvert the core stress granule component G3BP1 to promote viral VPg-dependent translation

Hosmillo

Jia

McAllaster

et al. 2019

Preprint

Self Cite

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“…It was initially hypothesized that the cell cycle arrest induced by NS5 was due to its known interaction with host eIF4G. The NS5 protein from several caliciviruses has been documented to aid in viral protein translation, through binding to several host eukaryotic initiation factors and recruiting ribosomes to the site of viral replication [11,30,[38][39][40]. The concentration of host eukaryotic initiation factors by VPg proteins is predicted to impair host translation [36].…”

Section: Discussionmentioning

confidence: 99%

Expression of the NS5 (VPg) Protein of Murine Norovirus Induces a G1/S Phase Arrest

Davies

Ward

2016

PLoS ONE

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Murine norovirus-1 (MNV-1) is known to subvert host cell division inducing an accumulation of cells in the G0/G1 phase, creating conditions where viral replication is favored. This study identified that NS5 (VPg), is capable of inducing cell cycle arrest in the absence of viral replication or other viral proteins in an analogous manner to MNV-1 infection. NS5 expression induced an accumulation of cells in the G0/G1 phase in an asynchronous population by inhibiting progression at the G1/S restriction point. Furthermore, NS5 expression resulted in a down-regulation of cyclin A expression in asynchronous cells and inhibited cyclin A expression in cells progressing from G1 to S phase. The activity of NS5 on the host cell cycle occurs through an uncharacterized function. Amino acid substitutions of NS5(Y26A) and NS5(F123A) that inhibit the ability for NS5 to attach to RNA and recruit host eukaryotic translation initiation factors, respectively, retained the ability to induce an accumulation of cells in the G0/G1 phase as identified for wild-type NS5. To the best of our knowledge, this is the first report of a VPg protein manipulating the host cell cycle.

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“…This interaction is required for translation of Feline calicivirus (FCV, genus Vesivirus, family Caliciviridae) RNA, so the VPg acts as a functional analog of the cap (Goodfellow et al, 2005;Hosmillo et al, 2014;Zhu et al, 2015). In contrast, the VPg on norovirus RNA binds and requires eIF4G for translation initiation (Chung et al, 2014). This difference in factor binding may be associated with the different structures of their VPgs.…”

Section: Canonical Translation Of Eukaryotic Mrnasmentioning

confidence: 99%

Non-canonical Translation in Plant RNA Viruses

et al. 2017

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Viral protein synthesis is completely dependent upon the host cell's translational machinery. Canonical translation of host mRNAs depends on structural elements such as the 5′ cap structure and/or the 3′ poly(A) tail of the mRNAs. Although many viral mRNAs are devoid of one or both of these structures, they can still translate efficiently using non-canonical mechanisms. Here, we review the tools utilized by positive-sense single-stranded (+ss) RNA plant viruses to initiate non-canonical translation, focusing on cis-acting sequences present in viral mRNAs. We highlight how these elements may interact with host translation factors and speculate on their contribution for achieving translational control. We also describe other translation strategies used by plant viruses to optimize the usage of the coding capacity of their very compact genomes, including leaky scanning initiation, ribosomal frameshifting and stop-codon readthrough. Finally, future research perspectives on the unusual translational strategies of +ssRNA viruses are discussed, including parallelisms between viral and host mRNAs mechanisms of translation, particularly for host mRNAs which are translated under stress conditions.

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Norovirus Translation Requires an Interaction between the C Terminus of the Genome-linked Viral Protein VPg and Eukaryotic Translation Initiation Factor 4G

Cited by 53 publications

References 50 publications

Noroviruses subvert the core stress granule component G3BP1 to promote viral VPg-dependent translation

Noroviruses subvert the core stress granule component G3BP1 to promote viral VPg-dependent translation

Expression of the NS5 (VPg) Protein of Murine Norovirus Induces a G1/S Phase Arrest

Non-canonical Translation in Plant RNA Viruses

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