Author: Myra Hosmillo; Jia Lu; Michael R. McAllaster; James B. Eaglesham; Xinjie Wang; Edward Emmott; Patricia Domingues; Yasmin Chaudhry; Timothy J Fitzmaurice; Matthew K.H. Tung; Marc Panas; Gerald McInerney; Nicholas Locker; Craig B. Willen; Ian Goodfellow
Title: Noroviruses subvert the core stress granule component G3BP1 to promote viral VPg-dependent translation Document date: 2019_3_8
ID: d0q5lhf4_43
Snippet: Therefore our data suggest that the interaction of VPg with G3BP1 is not direct, 447 fitting with our observation that this interaction is reduced by mutations in the eIF4G 448 binding domain (Fig 1A and Fig 9B. ) While our data fit with a primary role for G3BP1 449 in norovirus translation, we are unable to exclude the possibility that G3BP1 plays 450 . CC-BY-NC 4.0 International license is made available under a The copyright holder for this pr.....
Document: Therefore our data suggest that the interaction of VPg with G3BP1 is not direct, 447 fitting with our observation that this interaction is reduced by mutations in the eIF4G 448 binding domain (Fig 1A and Fig 9B. ) While our data fit with a primary role for G3BP1 449 in norovirus translation, we are unable to exclude the possibility that G3BP1 plays 450 . CC-BY-NC 4.0 International license is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. VPg-containing complexes again fits with our hypothesis that G3BP1 plays a role in 460 promoting viral VPg-dependent protein synthesis. 461
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