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ProteomicsInfluenza A hemagglutinin glycoproteomics similarity
Influenza A virus (IAV) mutates rapidly, preventing a single seasonal vaccine from targeting more than one strain, and year-to-year vaccine effectiveness is low. One challenge in designing effective vaccines is that genetic mutations frequently cause amino acid variations in IAV envelope protein hem...
ORGANISM(S): Viruses Homo sapiens (Human) Gallus gallus (Chicken) 
2020-07-03 | PXD018920 | Pride
Glycosylation Influenza a Lc-ms Similarity Glycopeptides 
ProteomicsImproving statistical certainty of glycosylation similarity between influenza A virus variants using data-independent acquisition mass spectrometry
The amino acid sequences of immunodominant domains of hemagglutinin (HA) on the surface of influenza A virus (IAV) evolve rapidly, producing viral variants. HA mediates receptor recognition, binding and cell entry, and serves as the target for IAV vaccines. Glycosylation, a post-translational modifi...
ORGANISM(S): Homo sapiens (Human) Canis familiaris (Dog) (Canis lupus familiaris) Gallus gallus (Chicken) 
2022-09-24 | PXD029700 | Pride
Influenza Dia Glycoproteomics Mass spectrometry Glycosylation similarity Hemagglutinin 
UnknownMeasuring Site-specific Glycosylation Similarity between Influenza a Virus Variants with Statistical Certainty.
Not available
S-EPMC8143645 | biostudies-literature
ProteomicsVariation of Site-Specific Glycosylation Profiles of Recombinant Influenza Glycoproteins
Recombinant proteins are of great interest in glycobiology and proteomics, known especially for their reproducibility and accessibility. However, variation in glycosylation among recombinant glycoproteins is not well understood and may depend on numerous conditions in the biomanufacturing process. I...
ORGANISM(S): Influenza A virus (A/California/04/2009(H1N1)) Influenza A virus (A/Thailand/1(KAN-1)/2004(H5N1)) Influenza A virus (A/Japan/305/1957(H2N2)) Influenza A virus (A/Netherlands/219/2003(H7N7)) Influenza A virus (A/Hong Kong/483/1997(H5N1)) Influenza A virus (A/New Caledonia/20/1999(H3N2)) Influenza A virus (A/Arizona/13/2008(H1N1)) Influenza A virus (A/Hong Kong/485197/2014(H3N2)) 
2024-08-13 | PXD042062 | Pride
Glycosylation Influenza a Site-specific Hemagglutinin 
ProteomicsSite-Specific Glycosylation Profiling of Protein Subunit and Inactivated Virus Vaccines
Many protein subunit vaccines and biologics contain glycosylated antigens and antibodies, yet quantitative frameworks for comparing glycosylation across lots, manufacturers, and production platforms remain limited. We performed site specific glycosylation LC-MS/MS analysis for intact N-linked glycop...
ORGANISM(S): Influenza A virus (A/Panama/2007/1999(H3N2)) Influenza A virus (A/Philippines/2/1982(H3N2)) Human alphaherpesvirus 3 Influenza A virus (A/New Caledonia/20/1999(H1N1)) Severe acute respiratory syndrome coronavirus 2 Influenza A virus (A/Shandong/9/1993(H3N2)) 
2026-07-21 | PXD074672 | Pride
Glycosylation Mass spectrometry Site-specific Vaccines Proteomics 
UnknownImproving Statistical Certainty of Glycosylation Similarity between Influenza A Virus Variants Using Data-Independent Acquisition Mass Spectrometry.
Not available
S-EPMC9593740 | biostudies-literature
TranscriptomicsMicroarray analysis of RNA of TCR transgenic CD8 T cells to assess the role of protein glycosylation in the decision between deletion vs. anergy in immune tolerance
Activation of peripheral T lymphocytes in the absence of pathogen induced inflammation or costimulatory signals results in tolerance. Two different tolerance mechanisms have been described, deletion and anergy. We recently demonstrated that an important variable which is responsible for the decisio...
ORGANISM(S): Mus musculus 
2011-09-07 | E-GEOD-31987 | biostudies-arrayexpress
ProteomicsChemical labeling for fine mapping of IgG N-glycosylation by ETD-MS
Immunoglobulin G (IgG), which contains four subclasses (IgG1-4), is one of the most important class of glycoproteins in immune system. Because of its importance in immune system, a steady increase of interest in developing IgG as biomarker or biotherapeutic agents for the treatment of diseases has b...
ORGANISM(S): Homo sapiens (Human) 
2019-08-26 | PXD014713 | Pride
Chemical labeling Igg Glycosylation Glycopeptides Electron transfer dissociation (etd) mass spectrometry 
UnknownDiscovery of genes required for lipoteichoic acid glycosylation predicts two distinct mechanisms for wall teichoic acid glycosylation.
Not available
S-EPMC5836110 | biostudies-literature
UnknownGlycosylation of bacterial antigens changes epitope patterns.
Not available
S-EPMC10637626 | biostudies-literature
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