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Identification and characterization of O-GlcNAc modifications of a conserved orthopoxvirus core protein

ABSTRACT: O-GlcNAcylation is a dynamic and reversible post-translational modification involving the attachment of a single β-N-acetylglucosamine (GlcNAc) moiety to the hydroxyl groups of serine or threonine residues. This modification occurs in thousands of cytoplasmic, nuclear, and mitochondrial proteins in mammalian cells and plays critical roles in regulating protein function, localization, and interactions. However, despite its widespread occurrence in host proteins, relatively few examples of O-GlcNAcylation have been reported in viral proteins. In this study, we sought to investigate the presence and functional relevance of O-GlcNAcylation in the vaccinia virus (VACV), a model poxvirus with a well-characterized replication cycle and virion architecture.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Vaccinia Virus Wr

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Yunliang Zhang

LAB HEAD: Bernard Moss

PROVIDER: PXD062753 | Pride | 2025-05-21

REPOSITORIES: Pride

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			Action	DRS
	A4_El_etdOT.mgf	Mgf
	A4_El_etdOT.myrimatch.mzid.gz	Mzid
	A4_El_etdOT.mzML	Mzml
	A4_El_etdOT.raw	Raw
	A4_chy_etd.mgf	Mgf

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Publications

Identification and characterization of O-GlcNAc modifications of a conserved orthopoxvirus core protein.

Zhang Yunliang Y Moss Bernard B

Journal of virology 20250523 6

O-GlcNAcylation, a post-translational modification consisting of O-linked N-acetylglucosamine attached to serine and threonine residues, occurs in thousands of cytoplasmic, nuclear, and mitochondrial proteins but has been reported for relatively few viral proteins. We used click chemistry, specific antibodies, and mass spectrometry to investigate the O-GlcNAcylation of vaccinia virus (VACV) proteins. A virion protein of ~40 kDa was identified by SDS-polyacrylamide gel electrophoresis following a ...[more]

PMID: 40407344

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Changes in gene expression within the skin caused by antigen-specific memory CD4+ T cells during Vaccinia virus infection.

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Site mapping of PGK1 O-GlcNAcylation

Project description:To identify the site(s) of O-GlcNAcylation on PGK1, we transiently co-expressed Flag-tagged PGK1 and OGT in HEK293T cells. After immunoprecipitation using anti-Flag M2 beads and in-gel trypsin digestion, resulted peptides were subjected to mass spectrometry analysis

2019-11-06 | PXD015659 | Pride

Next generation unnatural monosaccharides reveal that ESRRBO GlcNAcylation enhances pluripotency of mouse embryonic stem cells

Project description:Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling. As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per O acetylated, which, however, can induce a long-overlooked side reaction, non enzymatic S-glycosylation. Herein, we develop1,3 di esterified N azidoacetylgalactosamine (GalNAz) as the next generation chemical reporters for metabolic glycan labeling. Both 1,3 di O-acetylated GalNAz (1,3-Ac2GalNAz) and1,3 di O propionylated GalNAz (1,3-Pr2GalNAz)exhibited high efficiency for labeling protein O-GlcNAcylation with no artificial S-glycosylation. Applying1,3 Pr2GalNAz in mouse embryonic stem cells (mESCs), we identified ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein. We showed that ESRRB O-GlcNAcylation is important for mESC self-renewal and pluripotency. Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 25 (Ser 25), which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.

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Profiling whole-tissue metabolic reprogramming during cutaneous poxvirus infection and clearance

Project description:Background Vaccinia virus (VACV) infection induces prominent changes in host cell metabolism. Little is known about the global metabolic reprogramming that takes place in the whole tissue during viral infection. Here, we performed an unbiased longitudinal metabolomics study in VACV-infected mice to investigate metabolic changes in the tissue during infection. We assessed metabolites in homogenized skin over time in the presence or absence of antigen-specific T cells using untargeted mass spectrometry. VACV infection induced several significant metabolic changes, including in the levels of nucleic acid metabolites (reflecting the impact of viral replication on the skin metabolome). Furthermore, monocyte- and antiviral T cell-produced metabolites, including itaconic acid, glutamine, and glutathione, were significantly increased following infection, highlighting the immune response’s contribution to the global skin metabolome. Additional RNA-Seq of infected skin tissue recapitulated transcriptional changes identified via metabolomics. Overall, our study reveals the metabolic balance of viral replication and the antiviral immune response in the skin and identifies metabolic pathways that could contribute to cutaneous poxvirus control in vivo.

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Selective modulation of cell surface proteins during vaccinia infection: a resource for identifying viral immune evasion strategies

Project description:The interaction between immune cells and virus-infected targets involves multiple plasma membrane (PM) proteins. A systematic study of PM protein modulation by vaccinia virus (VACV), the paradigm of host regulation, has the potential to reveal not only novel viral immune evasion mechanisms, but also novel factors critical in host immunity. Here, >1000 PM proteins were quantified throughout VACV infection, revealing selective downregulation of known T and NK cell ligands including HLA-C, downregulation of cytokine receptors including IFNAR2, IL-6ST and IL-10RB, and rapid inhibition of expression of certain protocadherins and ephrins, candidate activating immune ligands. Downregulation of most PM proteins occurred via a proteasome-independent mechanism. Upregulated proteins included a decoy receptor for TRAIL. Twenty VACV-encoded PM proteins were identified, of which five were not recognised previously as such. Collectively, this dataset constitutes a valuable resource for future studies on antiviral immunity, host-pathogen interaction, poxvirus biology, vector-based vaccine design and oncolytic therapy.

2022-06-01 | PXD033407 | Pride

GATAD2B O-GlcNAcylation regulates breast cancer stem-like potential and drug resistance

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O-GlcNAc pattern of sOGT regulates its substrate selectivity and function

Project description:O-GlcNAcylation occurs on thousands of proteins involved in various cellular events. O-GlcNAc transferase (OGT), one of the enzymes responsible for protein O-GlcNAcylation, is known to be auto-O-GlcNAcylated at multiple sites. However, the role of O-GlcNAcylation on OGT is still unknown. Here, we report the role of O-GlcNAcylation on short form OGT (sOGT). By LC-ETD-MS analysis and western blot, we show that sOGT was mainly O-GlcNAcylated in the tetratricopeptide repeat (TPR) motifs with T12 and S56 being two “key” sites. T12 was a predominant O-GlcNAcylation site and the absence of S56 O-GlcNAcylation enhanced sOGT O-GlcNAcylation level. We found that O-GlcNAcylation of sOGT did not affect the enzyme activity but increased its binding to substrate proteins. S56A bound to and hence glycosylated more proteins, while T12A associated with fewer substrates. Proteomic studies combined with cell proliferation/cell cycle analyses indicated that S56A substantially enhanced cell proliferation, while T12A reduced it, and T12A led to a G2/M cell cycle arrest, due to O-GlcNAcylation of diverse proteins. These findings demonstrate that the O-GlcNAc pattern on sOGT modulates its function in cells by targeting different proteins.

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