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SARS-CoV-2 QTQTN motif mutant PTM-peptide mapping

ABSTRACT: 3 strains of SARS-CoV-2 were created to the function of the QTQTN motif adjacent to the Furin cleavage site on Spike protein: WT (QTQTN), Mutant 1 (QTQVN), Mutant 2 (QVQVN).

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Cercopithecus Aethiops (green Monkey) (grivet)

TISSUE(S): Cell Culture, Fibroblast

DISEASE(S): Severe Acute Respiratory Syndrome

SUBMITTER: Aaron Bailey

LAB HEAD: Vineet D. Menachery

PROVIDER: PXD034332 | Pride | 2022-07-20

REPOSITORIES: Pride

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Characterisation of the transcriptome and proteome of SARS-CoV-2 using direct RNA sequencing and tandem mass spectrometry reveals evidence for a cell passage induced in-frame deletion in the spike glycoprotein that removes the furin-like cleavage site.

Project description:Direct RNA sequencing using an Oxford Nanopore MinION characterised the transcriptome of SARS-CoV-2 grown in Vero E6 cells. This cell line is being widely used to propagate the novel coronavirus. The viral transcriptome was analysed using a recently developed ORF-centric pipeline. This revealed the pattern of viral transcripts, (i.e. subgenomic mRNAs), generally fitted the predicted replication and transcription model for coronaviruses. A 24 nt in-frame deletion was detected in subgenomic mRNAs encoding the spike (S) glycoprotein. This feature was identified in over half of the mapped transcripts and was predicted to remove a proposed furin cleavage site from the S glycoprotein. This motif directs cleavage of the S glycoprotein into functional subunits during virus entry or exit. Cleavage of the S glycoprotein can be a barrier to zoonotic coronavirus transmission and affect viral pathogenicity. Allied to this transcriptome analysis, tandem mass spectrometry was used to identify over 500 viral peptides and 44 phosphopeptides, covering almost all of the proteins predicted to be encoded by the SARS-CoV-2 genome, including peptides unique to the deleted variant of the S glycoprotein. Detection of an apparently viable deletion in the furin cleavage site of the S glycoprotein reinforces the point that this and other regions of SARS-CoV-2 proteins may readily mutate. This is of clear significance given the interest in the S glycoprotein as a potential vaccine target and the observation that the furin cleavage site likely contributes strongly to the pathogenesis and zoonosis of this virus. The viral genome sequence should be carefully monitored during the growth of viral stocks for research, animal challenge models and, potentially, in clinical samples. Such variations may result in different levels of virulence, morbidity and mortality.

2020-03-31 | PXD018241 | Pride

SARS-CoV-2 S protein ACE2 interaction reveals novel allosteric targets

Project description:SARS-CoV-2 spike protein binding to receptor ACE2 allosterically enhances furin proteolysisat distal S1/S2 cleavage sites

2021-08-09 | PXD023138 | Pride

Transcription profiling of mouse naive T cells isolated from CD4+ CD62L+ CD44- T cells were isolated from Fur flox/flox and CD4 cre Fur flox/flox mice reveals T cell-expressed proprotein convertase furin is essential for maintenance of peripheral tolerance

Project description:Furin is a proprotein convertase induced in activated T cells, reported to processes the anti-inflammatory cytokine TGFb-1. Herein, we show that conditional deletion of furin in T cells allowed for normal T cell development but impaired the function of regulatory T cells and effector cells, which produced less TGFb-1. Furin-deficient Treg cells, were less protective in a T cell transfer colitis model and failed to induce Foxp3 in normal T cells. Furin-deficient effector cells were inherently overly active and were resistant to suppressive activity of wild-type Tregs. Thus, our results indicate that furin is indispensable in maintaining peripheral tolerance, which is due, at least in part, to its nonredundant, essential function in regulating TGFb-1 production. Targeting furin has emerged as a strategy in malignant and infectious disease. The current work suggests that inhibiting furin might activate immune responses, but may result in a breakdown in peripheral tolerance. Experiment Overall Design: Naive CD4+ CD62L+ CD44- T cells were isolated from Fur flox/flox and CD4 cre Fur flox/flox mice. Replicated samples were achieved for wild type and knockout conditions.

2008-10-21 | E-GEOD-11884 | biostudies-arrayexpress

<i>PTMphinder</i>: an R package for PTM site localization and motif extraction from proteomic datasets.

Project description: Not available

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IgG purification- MS analysis - MS analysis was undertaken on human IgG purified using different approaches to assess purifity and potential alterations within the IgG N-linked glycans

Project description:MS analysis was undertaken on human IgG purified using different approaches to assess purifity and potential alterations within the IgG N-linked glycans

2019-11-01 | PXD014235 | Pride

Myeloid Cell Expressed Proprotein Convertase FURIN Attenuates Inflammation

Project description:The proprotein convertase enzyme FURIN processes immature pro-proteins into functional end- products. FURIN is upregulated in activated immune cells and it regulates T-cell dependent peripheral tolerance and the Th1/Th2 balance. FURIN also promotes the infectivity of pathogens by activating bacterial toxins and by processing viral proteins. Here, we evaluated the role of FURIN in LysM+ myeloid cells in vivo. Mice with a conditional deletion of FURIN in their myeloid cells (LysMCre-fur(fl/fl)) were healthy and showed unchanged proportions of neutrophils and macrophages. Instead, LysMCre-fur(fl/fl) mice had elevated serum IL-1β levels and reduced numbers of splenocytes. An LPS injection resulted in accelerated mortality, elevated serum pro-inflammatory cytokines and upregulated numbers of pro-inflammatory macrophages. A genome-wide gene expression analysis revealed the overexpression of several pro-inflammatory genes in resting FURIN-deficient macrophages. Moreover, FURIN inhibited Nos2 and promoted the expression of Arg1, which implies that FURIN regulates the M1/M2-type macrophage balance. FURIN was required for the normal production of the bioactive TGF-β1 cytokine, but it inhibited the maturation of the inflammation-provoking TACE and Caspase-1 enzymes. In conclusion, FURIN has an anti-inflammatory function in LysM+ myeloid cells in vivo.

2016-12-30 | GSE84117 | GEO

Furin deficiency efect on T cells

Project description:Analysis of T-cells lacking the proprotein convertase furin. Proprotein convertases promote the proteolytic maturation of proproteins. Furin is induced in activated T-cells. Results provide insight into the function of furin in T-cells. CD4+CD62L+CD44- naive, CD4+CD62L-CD44+ memory and CD4+CD25+FoxP3+ regulatory T cells were isolated from Fur flox/flox and CD4 cre Fur flox/flox mice. Naive T cells were activated via TCR. Total RNA was extracted from all cells and hybridized to Affymetrix microarrays.

2015-08-05 | E-GEOD-67884 | biostudies-arrayexpress

Furin deficiency effect on T cells

2015-08-05 | GSE67884 | GEO

T cell-expressed proprotein convertase furin is essential for maintenance of peripheral tolerance

2008-06-26 | GSE11884 | GEO

Common and strain-specific post-translational modifications of the potyvirus Plum pox virus coat protein in different hosts

Project description:Phosphorylation and O-GlcNAcylation are widespread post-translational modifications (PTMs) often sharing protein targets. Numerous studies have reported phosphorylation of plant virus proteins. In plants, research on O-GlcNAcylation lags behind regarding other eukaryotes and information about O-GlcNAcylated plant viral proteins is extremely scarce. The potyvirus Plum pox virus (PPV) causes sharka disease in Prunus trees, and also infects a wide range of experimental hosts. Capsid protein (CP) from virions of the PPV-R isolate purified from herbaceous plants can be extensively modified by O-GlcNAcylation and phosphorylation. In this study, a combination of proteomics and biochemical approaches has been employed to broaden knowledge of PPV CP PTMs. CP proved to be modified regardless it is assembled or not in mature particles. PTMs of CP occur in the natural host Prunus persica, similar to what happens in herbaceous plants. Additionally, we observe O-GlcNAcylation and phosphorylation are general features of different PPV strains, suggesting that roles of these modifications are part of overall strategies deployed during plant-virus interactions. Interestingly, phosphorylation at a casein kinase II motif conserved among potyviral CPs exhibits strain specificity in PPV; however, it does not display the critical role attributed to same modification in the CP of another potyvirus, Potato virus A.

2020-05-27 | PXD017780 | Pride

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