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J Mol Biol. 2017 Oct 27;429(21):3334-3352. doi: 10.1016/j.jmb.2017.04.007. Epub 2017 Apr 20.

The NS1 Protein from Influenza Virus Stimulates Translation Initiation by Enhancing Ribosome Recruitment to mRNAs.

Author information

1
CIRI, International Center for Infectiology Research, Université de Lyon, 69364 Lyon, France; Inserm, U1111, 69364 Lyon, France; Ecole Normale Supérieure de Lyon, 69364 Lyon, France; Université Lyon 1, Centre International de Recherche en Infectiologie, 69364 Lyon, France; CNRS, UMR5308, 69364 Lyon, France.
2
CIRI, International Center for Infectiology Research, Université de Lyon, 69364 Lyon, France; Inserm, U1111, 69364 Lyon, France; Ecole Normale Supérieure de Lyon, 69364 Lyon, France; Université Lyon 1, Centre International de Recherche en Infectiologie, 69364 Lyon, France; CNRS, UMR5308, 69364 Lyon, France; Laboratoire de Virologie et Pathologie Humaine VirPath, Université Claude Bernard Lyon 1, Hospices Civils de Lyon, Faculté de médecine RTH Laennec, rue Guillaume Paradin, F-69008 Lyon, France.
3
CIRI, International Center for Infectiology Research, Université de Lyon, 69364 Lyon, France; Inserm, U1111, 69364 Lyon, France; Ecole Normale Supérieure de Lyon, 69364 Lyon, France; Université Lyon 1, Centre International de Recherche en Infectiologie, 69364 Lyon, France; CNRS, UMR5308, 69364 Lyon, France. Electronic address: tohlmann@ens-lyon.fr.

Abstract

The non-structural protein NS1 of influenza A viruses exerts pleiotropic functions during infection. Among these functions, NS1 was shown to be involved in the control of both viral and cellular translation; however, the mechanism by which this occurs remains to be determined. Thus, we have revisited the role of NS1 in translation by using a combination of influenza infection, mRNA reporter transfection, and in vitro functional and biochemical assays. Our data show that the NS1 protein is able to enhance the translation of virtually all tested mRNAs with the exception of constructs bearing the Dicistroviruses Internal ribosome entry segment (IRESes) (DCV and CrPV), suggesting a role at the level of translation initiation. The domain of NS1 required for translation stimulation was mapped to the RNA binding amino-terminal motif of the protein with residues R38 and K41 being critical for activity. Although we show that NS1 can bind directly to mRNAs, it does not correlate with its ability to stimulate translation. This activity rather relies on the property of NS1 to associate with ribosomes and to recruit them to target mRNAs.

KEYWORDS:

NS1; RNA; influenza; ribosome; translation

PMID:
28433538
DOI:
10.1016/j.jmb.2017.04.007
[Indexed for MEDLINE]

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