Browse
Submit Data
Databases
API
Help

Dataset Information

474 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Quantitative proteomic analysis of Murine Norovirus infected BV-2 cells (v2)

ABSTRACT: SILAC-labelling analysis of murine BV-2 cells infected at high multiplicity of infection (10 TCID50/cell) and harvested at 4h or 9h post-infection. Represents the first quantitative proteomics analysis of norovirus-infected cells. A paired AP-MS dataset investigates the effects of MNV infection on eukaryotic initiation factor (eIF) complex formation with this dataset providing data on the overall abundance of eIF components in infected cells. This is a reanalysis of an earlier dataset (PXD004015) performed in Maxquant (v1.5.5.1).

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Dendritic Cell, Cell Culture

SUBMITTER: Edward Emmott

LAB HEAD: Ian Goodfellow

PROVIDER: PXD004984 | Pride | 2017-01-17

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Publications

Norovirus-Mediated Modification of the Translational Landscape via Virus and Host-Induced Cleavage of Translation Initiation Factors.

Emmott Edward E Sorgeloos Frederic F Caddy Sarah L SL Vashist Surender S Sosnovtsev Stanislav S Lloyd Richard R Heesom Kate K Locker Nicolas N Goodfellow Ian I

Molecular & cellular proteomics : MCP 20170113 4 suppl 1

Noroviruses produce viral RNAs lacking a 5' cap structure and instead use a virus-encoded viral protein genome-linked (VPg) protein covalently linked to viral RNA to interact with translation initiation factors and drive viral protein synthesis. Norovirus infection results in the induction of the innate response leading to interferon stimulated gene (ISG) transcription. However, the translation of the induced ISG mRNAs is suppressed. A SILAC-based mass spectrometry approach was employed to analy ...[more]

PMID: 28087593

Similar Datasets

Quantitative proteomic analysis of Murine Norovirus infected BV-2 cells

Project description:SILAC-labelling analysis of murine BV-2 cells infected at high multiplicity of infection (10 TCID50/cell) and harvested at 4h or 9h post-infection. Represents the first quantitative proteomics analysis of norovirus-infected cells. A paired AP-MS dataset investigates the effects of MNV infection on eukaryotic initiation factor (eIF) complex formation with this dataset providing data on the overall abundance of eIF components in infected cells.

2016-06-28 | PXD004015 | Pride

AP-MS analysis of m7GTP-binding proteins in Murine norovirus infected BV-2 cells (v2)

Project description:SILAC-labelling analysis of murine BV-2 cells infected at high multiplicity of infection (10 TCID50/cell) and harvested at 4h or 9h post-infection. Lysates were then suject to m7GTP-sepharose affinity purification to enrich for translation initiation factors. As norovirus translation uses a VPg protein covalently linked to the 5' of its RNAs for initiation factor recruitment it was hypothesised that norovirus infection could modify initiation factor complexes. A paired dataset investigates the effects of MNV infection on total protein levels in infected cells. This dataset is a Maxquant reanalysis of data previously submitted under PXD004019

2017-01-17 | PXD004983 | Pride

AP-MS analysis of m7GTP-binding proteins in Murine norovirus infected BV-2 cells

Project description:SILAC-labelling analysis of murine BV-2 cells infected at high multiplicity of infection (10 TCID50/cell) and harvested at 4h or 9h post-infection. Lysates were then suject to m7GTP-sepharose affinity purification to enrich for translation initiation factors. As norovirus translation uses a VPg protein covalently linked to the 5' of its RNAs for initiation factor recruitment it was hypothesised that norovirus infection could modify initiation factor complexes. A paired dataset investigates the effects of MNV infection on total protein levels in infected cells (PXD004015).

2016-07-07 | PXD004019 | Pride

Phosphoproteomic analysis of Bluetongue virus infection

Project description:Bluetongue virus causes infections in wild and domesticated ruminants, with the potential for causing significant morbidity, mortality and economic harm in both the developing and developed world. While vaccines have been developed, no treatment for acute infections exists. In this regard, a possible approach is to determine host-cell factors utilised by Bluetongue virus. We thus proceeded to characterize the phosphoproteome of BTV infected HeLa cells to elucidate the intracellular signalling pathways and identify critical host factors activated during Bluetongue virus infection.

2017-08-29 | PXD005550 | Pride

Identification of hypoxia-induced proteins using SILAC-based proteomics

Project description:A hallmark of solid tumours is the development of hypoxic regions where rapidly growing transformed cells outstrip their blood supply. Tumour cells in these starved regions sense reduced levels of oxygen and switch on genes that help them to adapt, survive and continue growing. Since hypoxia is a key physiological difference between normal and cancer tissue, an opportunity exists to selectively kill tumour cells by exploiting the differences in protein expression between normal and hypoxic tumour tissue. However, a major challenge is to identify druggable hypoxia-induced proteins critical for tumour cell survival. This is especially important in cancers of unmet need where hypoxia gene signatures correlate with poor prognosis (for example, colorectal cancers). To identify new hypoxia-induced proteins, we performed SILAC-based proteomics on colorectal cancer cells exposed to normoxia and hypoxia. In this study, we identify a new hypoxia-activated GPCR signalling axis that enables colorectal tumour cells to survive the microenvironmental stress of hypoxia. Our findings uncover a previously unappreciated role for this GPCR-axis as a key regulator of the adaptive response to hypoxia and highlght an opportunity to exploit tumour-associated hypoxia for therapy.

2018-09-18 | PXD009971 | Pride

ChAdOx infection of human cell lines A549 MRC-5

Project description:Total proteome and phospho proteome of two human cell lines infected with the ChAdOx1 nCoV-19 virus over 72 hours

2021-01-11 | PXD023286 | Pride

Mass spectrometry of immunoprecipitations from control and Er blood group

Project description:Immunoprecipitates were prepared from test Er(a+b-) donor RBCs and negative control Er(a-b+) (P1) RBCs using anti-Era plasma from P3 (5:1 ratio of plasma to cells) and proteomic analysis was performed.

2024-01-26 | PXD035013 | Pride

Human Platelet PIP3 Signalosome

Project description:Platelets are small, anucleate cells that play an essential role in haemostasis, but can contribute critically to the pathogenesis of cardiovascular disease. Platelets express all four Class I Phosphoinositide 3-kinase (PI3K) isoforms, with previous work revealing important roles for these enzymes in regulating platelet priming, activation and stable thrombus formation. Despite this, detailed mechanistic understanding of how these lipid kinases orchestrate these roles in platelets is limited. Class I PI3Ks predominantly regulate cell function through their catalytic product, the signalling phospholipid phosphatidylinositol-3,4,5-trisphosphate (PIP3), which coordinates the localisation and/or activity of a diverse range of binding proteins. The complete repertoire of these Class I PI3K effectors in platelets remains unknown, hampering current understanding of Class I PI3K-mediated regulation of platelet function. We therefore conducted a global, unbiased screen for PIP3-binding proteins in human platelets using affinity capture coupled to high resolution proteomic mass spectrometry. Thus, we present the first in depth analysis of the PIP3 signalosome of human platelets, revealing an extensive PIP3 interactome, including many proteins previously uncharacterised in this cell type. This work provides important new insights into how Class I PI3K shapes human platelet function.

2017-06-06 | PXD003777 | Pride

A novel paracrine induction of RNA Granules by Feline Calicivirus

Project description:We are here presenting a new paracrine induction of RNA granules by viruses. Infection by viruses imposes major stress on the host cell. In response to this stress, infected cells can induce several defence mechanisms, which include the activation of stress response pathways and the innate immune response. These often result in an inhibition of translation culminating in the assembly of cytoplasmic granules called stress granules (SGs). SGs assembly follows from liquid phase separation of aggregation-prone proteins such G3BP1 and TIA-1, leading to the sequestration of mRNAs. Because this threatens viral gene expression, viruses need to evade these stress response pathways to propagate. Using feline calicivirus (FCV), surrogate for norovirus, the main virus responsible for gastroenteritis outbreaks worldwide, we previously showed that FCV impairs SGs assembly by cleaving the scaffold protein G3BP1. Interestingly, we observed that uninfected bystander cells assembled G3BP1 granules, suggesting a paracrine response trigged by the infection. We now present evidence that virus-free supernatant generated from infected cells can induce the formation of RNA granules. We have characterised the dynamic of the granules assembly via confocal microscopy. Moreover, we provide an understanding of paracrine granules function and specificity through their affinity purification followed by proteomics and RNAseq analysis of their proteins and mRNAs content. This helps to define rules of assembly and novel functions for paracrine granules highlighting fundamental differences with canonical stress granules.

2022-03-14 | PXD021881 | Pride

Respiratory Health Outcomes in Neonates (RHiNO) Study Urine Proteomics

Project description:Urine sampled from preterm-born (<34 weeks gestation) school-aged (7-12yrs) children and term born (>/=37 weeks gestation). Spirometry, exercise testing and cardiovascular assessment performed at time of sampling. Preter-born children with low lung function entered a randomised placebo controlled trial of inhaler therapies.

2023-07-31 | PXD042759 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data