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

ABSTRACT: 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)

ORGANISM(S): Danio rerio

PROVIDER: GSE49626 | GEO | 2013/08/08

SECONDARY ACCESSION(S): PRJNA214512

REPOSITORIES: GEO

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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

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

Use of an immune-specific microarray for identifying transcriptome profiles associated to VHSV infection or vaccination with a G gene- DNA vaccine in turbot (Scophthalmus maximus)

Project description:With the aim of shedding light on the protection conferred by the DNA vaccines based in the G glycoprotein of viral haemorrhagic septicaemia virus (VHSV) in turbot (Scophthalmus maximus) we have used a specific microarray highly enriched in antiviral sequences to carry out the transcriptomic study associated to VHSV DNA vaccination/infection. The differential gene expression pattern in response to empty plasmid (pMCV1.4) and DNA vaccine (pMCV1.4-G860) intramuscular administration with regard to non-stimulated turbot was analyzed in head kidney at 8, 24 and 72 hours post-vaccination. Moreover, the effect of VHSV infection one month after immunization was also analyzed in vaccinated and non-vaccinated fish at the same time points.

2015-04-01 | GSE56487 | GEO

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

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

| PRJNA535512 | ENA

Filariasis test strip (FTS) antibody recognition of Brugia malayi glycoproteins

Project description:Rapid and accurate prevalence mapping of lymphatic filariasis (LF) is necessary to eliminate this disfiguring and disabling neglected tropical disease. Unfortunately, rapid tests such as the filariasis test strip (FTS) for Wuchereria bancrofti, the causative agent of LF in Africa, can cross-react with antigens circulating in some persons infected by the African eye worm, Loa loa, rendering the test unreliable in eleven co-endemic nations. The intended target of the FTS is a heavily glycosylated W. bancrofti circulating filarial antigen (Wb-CFA). Previously, we determined that the FTS monoclonal antibody, AD12.1, which detects a carbohydrate epitope on Wb-CFA, also detects multiple L. loa proteins in cross-reactive sera from persons with loiasis. Since the carbohydrate epitope recognized by AD12.1 is present on glycoproteins of other parasitic nematodes, including Brugia species, it is unclear why reactive glycoproteins are not detected in infections with other filarial parasites. To gain a better understanding of the proteins recognized by the FTS diagnostic antibody, we used proteomics and to characterize filarial glycoproteins that are bound by the AD12.1 antibody using Brugia malayi as a model. This included using shotgun proteomics to catalog the AD12-reactive glycoproteins found in adult female somatic (BmSOM) and excretory/secretory (BmES) antigens. As well as in-gel proteomics of two predominant protein bands from BmES.

2023-09-28 | PXD027003 | Pride

N-GlycositeAtlas, a database resource for mass spectrometry-based human N-linked glycoproteins and glycosylation sites

Project description:N-Linked glycoprotein is a highly interesting class of proteins for clinical and biological research. The large-scale characterization of N-linked glycoproteins accomplished by mass spectrometry-based glycoproteomics has provided valuable insights into the interdependence of glycoprotein structure and protein function. However, these studies focus mainly on the analysis of specific sample type, and lack integration of each glycoproteomic data from different tissues, body fluids or cell types. In this study, we established N-GlycositeAtlas, a comprehensive database resource of human N-linked glycoproteins and their glycosylation sites identified by mass spectrometry. N-GlycositeAtlas contains more than 30,000 glycosite-containing peptides (representing >14,000 N-glycosylation sites) from more than 7,000 N-glycoproteins from different biological sources including human-derived tissues, body fluids and cell lines from over 100 studies. The entire human N-glycoproteome database as well as 22 sub-databases associated with individual tissues or body fluids can be downloaded from the N-GlycositeAtlas website at nglycositeatlas.biomarkercenter.org.

2019-11-08 | PXD005143 | Pride

N-GlycositeAtlas, a database resource for mass spectrometry-based human N-linked glycoproteins and glycosylation sites

2022-02-23 | PXD005232 | Pride

A pipeline for discovery and verification of glycoproteins from plasma-derived extracellular vesicles as breast cancer biomarkers

Project description:Glycoproteins comprise more than half of current FDA-approved protein cancer markers but the development of new glycoproteins as disease biomarkers has been stagnant. Here we present a pipeline to develop glycoproteins from extracellular vesicles (EVs) through integrating quantitative glycoproteomics with a novel reverse phase glycoprotein array, and then apply it to identify novel biomarkers of breast cancer. EV glycoproteomics show promise in circumventing the problems plaguing current serum glycoproteomics and allowed us to identify hundreds of glycoproteins that have not been identified in serum. We identified 1,453 unique glycopeptides representing 556 glycoproteins in EVs, among which 20 are significantly higher in breast cancer patients. We further applied a novel glyco-specific reverse phase protein array to quantify a subset of the candidates. Together, this study demonstrates the great potential of this integrated pipeline for biomarker discovery.

2018-04-26 | PXD007572 | Pride

Analysis of the glycoproteins present on Fasciola hepatica surface tegument

Project description:Fasciola hepatica, commonly known as liver fluke, is a trematode which causes Fasciolosis in ruminants and humans. The outer tegumental coat of F. hepatica is a complex metabolically active biological matrix that is continually exposed to the host immune system. It is highly glycosylated and parasite-derived immunogenic oligosaccharide motifs and glycoproteins are currently being investigated as novel vaccine candidates. We selectively enriched for FhTeg mannosylated glycoprotein subsets using lectin affinity chromatography and identified 369 proteins by mass spectrometric analysis.

2016-08-03 | PXD003911 | Pride

Whole-Cell Cancer Vaccines Induce Large Antibody Responses to Carbohydrates and Glycoproteins

Project description:Purpose: This study uses a high-throughput glycan microarray to profile anti-glycan immune responses to whole-cell vaccines: GVAX Pancreas, K562-GM and H1299. The aim was to indentify anti-glycan antibody responses relevent to patient clinical outcomes Results: Immune responses to non-human antigens bovine fetuin and alpha-Gal antigens were identified induced by GVAX Pancreas. The magnitude of these responses inversely correlate with patient survival. The non-human antigens were likely incorporated from cell media used for vaccine production. Their presence distracted immune system, resulting in decreased immune response to vaccine antigens. Conclusion: This study highlighted the importance of anti-glycan immune response in vaccine development. Whole-cell vaccinesderived from human cell lines could incorporate non-human antigens from cell media. These xeno-antigens may have negative impact on the vaccine efficacy.

2016-12-13 | GSE83087 | GEO

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