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AP-MS analysis of FLAG-tagged Murine norovirus (NS1/2 and NS4)

ABSTRACT: Norovirus replication is accomplished by the use of a number of viral proteins derived from a long polyprotein. These components are named from NS1/2 to NS7. Having previously determined that the incorporation of FLAG epitope tags into certain positions in the norovirus genome was tolerated (Thorne et. al. 2012 J. Virol)

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Ssrna Viruses Mus Musculus (mouse)

TISSUE(S): Cell Culture, Macrophage

SUBMITTER: Edward Emmott

LAB HEAD: Ian Goodfellow

PROVIDER: PXD011779 | Pride | 2019-09-09

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	290416_Flag_Exp1.raw	Raw
	290416_Flag_Exp2.raw	Raw
	290416_Flag_Exp3.raw	Raw
	MNV_FLAG_NS12_NS4.zip	Other
	MNVseparatedpolyprotein.fasta	Fasta

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1 - 5 of 6

Publications

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

Hosmillo Myra M Lu Jia J McAllaster Michael R MR Eaglesham James B JB Wang Xinjie X Emmott Edward E Domingues Patricia P Chaudhry Yasmin Y Fitzmaurice Tim J TJ Tung Matthew Kh MK Panas Marc Dominik MD McInerney Gerald G Locker Nicolas N Wilen Craig B CB Goodfellow Ian G IG

eLife 20190812

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]

PMID: 31403400

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AP-MS analysis of murine and human norovirus VPg interactomes

Project description: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.

2019-09-09 | PXD007585 | Pride

JEV NS1'-interacting cellular proteins

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Selective polyprotein processing determines norovirus sensitivity to Trim7

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mRNA display with library of even-distribution reveals cellular interactors of influenza virus NS1

Project description:The interactome of Influenza (A/WSN/33) NS1 protein (WT and D92Y mutant) was identifiedy by AP-MS.

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NS1-mediated inhibition of c-Abl results in acute lung injury and priming for bacterial co-infections; insights into 1918 H1N1 pandemic

Project description:NS1 proteins from avian influenza viruses like the 1918 pandemic NS1 are capable of inhibiting the key signaling integrator c-Abl (Abl1), resulting in massive cytopathic cell alterations. In the current study, we addressed the consequences of NS1-mediated alteration of c-Abl on acute lung injury and pathogenicity. Comparing isogenic strains that differ only in their ability to inhibit c-Abl, we observed elevated pathogenicity for the c-Abl-inhibiting virus. NS1-mediated block of c-Abl resulted in severe lung pathology and massive edema formation and facilitated secondary bacterial pneumonia. This phenotype was independent of differences in replication and immune responses, defining it as an NS1 virulence mechanism distinct from its canonical functions. Microarray analysis revealed extensive down-regulation of genes involved in cell integrity and vascular endothelial regulation. In conclusion, NS1 protein-mediated blockade of c-Abl signaling drives acute lung injury and primes for bacterial co-infections revealing potential insights into the pathogenicity of the 1918 pandemic virus. Lung transcription analysis of Influenza A virus infected mice.

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Dengue Virus NS1 Replicon - Dengue virus (DENV) is a major human pathogen that belongs to the flavivirus genus

Project description:Dengue virus (DENV) is a major human pathogen that belongs to the flavivirus genus. Among non-structural viral proteins, NS1 is an enigmatic factor that is exclusively encoded by members of the flavivirus genus within the Flaviviridae family and accomplishes different functions during DENV infection. To gain insight into the molecular and cellular function of NS1 in viral replication, we generated a tagged NS1 DENV replicon and identified the associated host proteins during active viral replication. Replicons are self-replicating flavivirus RNAs containing large in-frame deletions in the structural genes and are useful tools to study translation and RNA amplification of several flaviviruses. To establish a global map of NS1-host protein interactions occurring during DENV replication, we stably expressed a DENV2 replicon encoding NS1 tagged with N-terminal FLAG and HA epitopes (FH-NS1) or the untagged version (WT) in three different human cell lines (Raji, HeLa and HAP1). Interactors of NS1 were identified by AP-MS/MS from these three different cell lines.

2017-11-29 | PXD008120 | Pride

Phosphoproteomic studies of role of LAR protein tyrosine phosphatase in mouse embryonic fibroblasts

Project description:To gain insights into the signalling pathways regulated by Leukocyte common antigen-related protein (LAR), including those that are PDGF-dependent, we have carried out the first systematic analysis of LAR-regulated signal transduction using SILAC-based quantitative proteomic and phosphoproteomic techniques. We have analysed differential phosphorylation between wild-type mouse embryo fibroblasts (MEFs) or MEFS in which the LAR cytoplasmic phosphatase domains had been deleted (LARΔP).

2016-04-15 | PXD002545 | Pride

The NS1 protein of influenza A virus suppresses interferon-regulated activation of antigen-presentation and immune-proteasome pathways

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NS1 protein of influenza A virus and interferon

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