Proteomics

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AP-MS analysis of murine and human norovirus VPg interactomes

ABSTRACT: The norovirus VPg protein is covalently linked to the viral genome in place of a 5' cap, and functions as a cap-substitute, capable of interacting with translation initiation factors. Following on from our previous study (Chung et. al. 2014, J. BIol. Chem.) we wished to determine the interactome of human norovirus VPg, and compare that of murine norovirus VPg. We had previously demonstrated that mutation of the penultimate C-terminal phenylalanine residue in murine norovirus VPg greatly reduced initiation factor binding (F123A). Insertion of the equivalent mutation into human norovirus (F137A) also reduced initiation factor binding. Affinity purification of wild-type of mutant human and murine norovirus VPg was accomplished using GFP-tagged VPg transfected into SILAC-labelled human HEK-293T cells.

INSTRUMENT(S): Orbitrap Fusion ETD, LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Hek-293t Cell

SUBMITTER: Edward Emmott  

LAB HEAD: Ian Goodfellow

PROVIDER: PXD007585 | Pride | 2019-09-09

REPOSITORIES: Pride

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20160422MNVNVVPgminusrequant.zip Other
220416_Exp1.raw Raw
220416_Exp2.raw Raw
220416_Exp3_NewSample.raw Raw
250714_Exp_1.raw Raw
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Publications

Knowledge of the host factors required for norovirus replication has been hindered by the challenges associated with culturing human noroviruses. We have combined proteomic analysis of the viral translation and replication complexes with a CRISPR screen, to identify host factors required for norovirus infection. The core stress granule component G3BP1 was identified as a host factor essential for efficient human and murine norovirus infection, demonstrating a conserved function across the <i>Nor  ...[more]

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