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Free glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast

ABSTRACT: Free glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast

PROVIDER: PRJNA535512 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8956970.fastq.gz	Fastqsanger.gz
	SRR8956971.fastq.gz	Fastqsanger.gz
	SRR8956972.fastq.gz	Fastqsanger.gz
	SRR8956973.fastq.gz	Fastqsanger.gz
	SRR8956974.fastq.gz	Fastqsanger.gz

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Free glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast

Project description:In eukaryotic cells, unconjugated oligosaccharides structurally related to N-glycans (FNGs) are generated either from misfolded N-glycoproteins destined for endoplasmic reticulum (ER)-associated degradation (ERAD), or from lipid-linked oligosaccharides, donor substrates for N-glycosylation of proteins. The mechanism responsible for the generation of FNGs is now well understood, but whether there are other type of free glycans remain unclarified. Here, we report on the accumulation of O-mannosylated free glycans in budding yeast that were cultured in media containing mannose as a carbon source. A structural analysis of these glycans revealed that their structures are identical to those of O-mannosyl glycans that are attached to glycoproteins. Deletion of the cyc8 gene, encoding a general transcription repressor, resulted in the accumulation of excessive amounts of the free O-glycans, concomitant with a severe growth defect, a reduction in the level of cellular O-mannosylated proteins, and compromised cell wall integrity. Our findings provide evidence for a regulated pathway for O-glycoprotein degradation in yeast and offer critical insights into the catabolic mechanisms that control the fate of O-glycosylated proteins.

2019-07-24 | GSE130332 | GEO

Free glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast.

Project description:In eukaryotic cells, unconjugated oligosaccharides that are structurally related to N-glycans (i.e. free N-glycans) are generated either from misfolded N-glycoproteins destined for the endoplasmic reticulum-associated degradation or from lipid-linked oligosaccharides, donor substrates for N-glycosylation of proteins. The mechanism responsible for the generation of free N-glycans is now well-understood, but the issue of whether other types of free glycans are present remains unclear. Here, we report on the accumulation of free, O-mannosylated glycans in budding yeast that were cultured in medium containing mannose as the carbon source. A structural analysis of these glycans revealed that their structures are identical to those of O-mannosyl glycans that are attached to glycoproteins. Deletion of the cyc8 gene, which encodes for a general transcription repressor, resulted in the accumulation of excessive amounts of free O-glycans, concomitant with a severe growth defect, a reduction in the level of an O-mannosylated protein, and compromised cell wall integrity. Our findings provide evidence in support of a regulated pathway for the degradation of O-glycoproteins in yeast and offer critical insights into the catabolic mechanisms that control the fate of O-glycosylated proteins.

| S-EPMC6827276 | biostudies-literature

Hydrophilic interaction chromatography coupled to ultraviolet photodissociation affords identification, localization, and relative quantitation of glycans on intact glycoproteins

Project description:Protein glycosylation is implicated in a wide array of diseases, yet glycoprotein analysis remains elusive owing to the extreme heterogeneity of glycans including microheterogeneity at the same amino acid residue (glycosite). Top-down mass spectrometry (MS) allows precise identification and localization of glycans on intact proteins, and coupling top-down MS with chromatography allows time-resolved characterization of glycoforms. Here, we couple ultraviolet photo-dissociation (UVPD) to hydrophilic interaction chromatography (HILIC) to advance the characterization of glycoproteins ranging from 15-34 kDa, offering site localization of glycans, providing sequence coverages up to 93% and relative quan-titation of individual glycoforms.

2024-02-24 | PXD050098 | JPOST Repository

Study of the differentially-expressed genes induced by the expession of two viral glycoproteins in muscle cells of adult zebrafish

Project description:A genomic approach was used to indentify the differences in the gene expression profiles of adult zebrafish injected with different viral glycoproteins. This study intended to study the mechanisms of immunogenicity of each glycoprotein (gpG of VHSV and SVCV) Fish were injected with plasmids encoding the different glycoproteins and muscle samples at the site of injection were compared to control samples at three days post-immunisation.

2013-08-08 | E-GEOD-49626 | biostudies-arrayexpress

Enhanced Quantitative LC-MS/MS Analysis of N-linked Glycans Derived from Glycoproteins Using Sodium Deoxycholate Detergent

Project description:Protein glycosylation is a common protein post-translational modification (PTM) in living organisms and has been shown to associate with multiple diseases, and thus may potentially be a biomarker of such diseases. Efficient protein/glycoprotein extraction is a key step in the preparation of N-glycans derived from glycoproteins prior to LC-MS analysis. Convenient, efficient and unbiased sample preparation protocols are needed. Herein, we evaluated the use of sodium deoxycholate (SDC) acidic labile detergent to release N-glycans of glycoproteins derived from biological samples such as cancer cell lines. Compared to the filter aided sample preparation approach, the sodium deoxycholate (SDC) assisted approach was determined to be more efficient and unbiased. SDC removal was determined to be more efficient when using acidic precipitation rather than ethyl acetate phase transfer. Efficient extraction of proteins/glycoproteins from biological samples was achieved by combining SDC lysis buffer and beads beating cell disruption. This was suggested by a significant overall increase in the intensities of N-glycans released from cancer cell lines. Additionally, the use of SDC approach was also shown to be more reproducible than those methods that do not use SDC.

2018-05-16 | PXD008687 | Pride

Mannose Receptor glycoprotein ligands in A549 cells

Project description:The macrophage mannose receptor (CD206, MR) is an endocytic lectin receptor which plays an important role in homeostasis and innate immunity. The MR contains C-type lectin domains (CTLD) whose specificity for endogenous glycans and glycoprotein ligands have not been well studied. To gain more insights into the recognition by the MR, we used the murine MR CTLD 4-7 coupled to the Fc-part of IgG (MR-Fc) to investigate its glycan and glycoprotein recognition. As lung cancer tissue and the lung cancer cell line A549 showed intense MR-Fc binding, we further investigated the MR glycoprotein ligands in those cells by immunoprecipitation and glycoproteomic analysis. All enriched glycoproteins, of which 42 were identified, contained pauci- or oligomannose N-glycans, confirming the microarray results. Our study demonstrates that the MR CTLD4-7 is highly selective for pauci- and oligomannosidic N-glycans, structures that are often elevated in tumor cells, and suggest a potential role for the MR in tumor biology.

2022-06-21 | PXD022546 | Pride

Study of the differentially-expressed genes induced by the expession of two viral glycoproteins in muscle cells of adult zebrafish

2013-08-08 | GSE49626 | GEO

Transcriptomic profiles of Streptococcus mutans UA159 grown in the presence or absence of mucins or mucin glycans

Project description:We use high-throughput sequencing to profile the response of oral commensal pathogen Streptococcus mutans to mucins protein polymers (human MUC5B mucins) and soluble mucin glycans (human MUC5B glycans and porcine MUC5AC glycans). We find that mucins and their glycans alter the regulation of dozens of S. mutans genes, specifically downregulating competence-associated quorum sensing genes. The transcriptional responses induced by MUC5B mucins, MUC5B glycans, and MUC5AC glycans are highly correlated.

2021-01-01 | GSE163258 | GEO

Ruminococcus torques is a keystone degrader of intestinal mucin glycoprotein, releasing oligosaccharides used by Bacteroides thetaiotaomicron

Project description:Symbiotic interactions between humans and our communities of resident gut microbes (microbiota) play many roles in health and disease. Some gut bacteria utilize mucus as a nutrient source and can under certain conditions damage the protective barrier it forms, increasing disease susceptibility. We investigated how Ruminococcus torques—a known mucin-degrader that remains poorly studied despite its implication in inflammatory bowel diseases (IBDs)— degrades mucin glycoproteins or their component O-linked glycans to understand its effects on the availability of mucin-derived nutrients for other bacteria. We found that R. torques utilizes both mucin glycoproteins and released oligosaccharides from gastric and colonic mucins, degrading these substrates with a panoply of mostly constitutively expressed, secreted enzymes. Investigation of mucin oligosaccharide degradation by R. torques revealed strong fucosidase, sialidase and b1,4-galactosidase activities. There was a lack of detectable sulfatase and weak β1,3-galactosidase degradation, resulting in accumulation of glycans containing these structures on mucin polypeptides. While the Gram-negative symbiont, Bacteroides thetaiotaomicron grows poorly on mucin glycoproteins, we demonstrate a clear ability of R. torques to liberate products from mucins, making them accessible to B. thetaiotaomicron. This work underscores the diversity of mucin-degrading mechanisms in different bacterial species and the probability that some species are contingent on others for the ability to more fully access mucin-derived nutrients. The ability of R. torques to directly degrade a variety of mucin and mucin glycan structures and unlock released glycans for other species suggests that it is a keystone mucin degrader, which may contribute to its association with IBD.

2024-06-19 | GSE262875 | GEO

A chemoenzymatic method for simultaneous profiling N- and O-glycans on glycoproteins using one-pot format

Project description:Glycosylation, including N-glycosylation and O-glycosylation is generally characterized and controlled as a critical quality attribute for therapeutic glycoproteins because glycans can impact protein-based drug product efficacy, half-life, stability, and safety. Analytical procedures to characterize N-glycans are relatively well-established, but the characterization of O-glycans is challenging due to the complex workflows and lack of enzymatic tools. Here we present a simplified chemoenzymatic method to simultaneously profile N- and O-glycans from the same sample using a one-pot format by mass spectrometry (MS). N-glycans were first released by PNGase F, followed by O-glycopeptide generation by Proteinase K, selective N-glycan reduction, and O-glycan release by β-elimination during permethylation of both N- and O- glycans. Glycan structural assignments, and determination of N- to O-glycan ratio was obtained from the one-pot mass spectra. The streamlined, one-pot method is an accurate and reproducible approach that will facilitate advanced characterizations for quality assessments of therapeutic glycoproteins.

2024-08-01 | PXD052172 | Pride

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