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ProteomicsMiddle-up analysis of polyclonal IgG-Fc
Middle-up strategy for the analysis of the fragment crystallizable (Fc) region of human plasma immunoglobulins G (IgGs). The use of hydrophilic interaction liquid chromatography (HILIC) and capillary electrophoresis (CE) coupled to mass spectrometry (MS) allowed to get a comprenhesive view of the N-...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-05-08 | MSV000085388 | MassIVE
ProteomicsIgG Fc Glycosylation of Total and Disease-Specific Autoantibodies in Systemic Sclerosis
This dataset contains IgG Fc glycosylation profiles of total and antigen-specific autoantibodies from systemic sclerosis (SSc) patients and healthy controls (n = 187). Total IgG and anti-centromere protein B (ACA) and anti-topoisomerase I (ATA) IgG were affinity-purified, digested with trypsin, and ...
ORGANISM(S): Homo sapiens (Human) 
2026-09-14 | PXD083619 | Pride
Human Autoantibodies Systemic sclerosis Lc-ms Plasma Igg fc glycosylation 
ProteomicsHuman IgG subclasses differ in structural elements of their N-glycosylation
We tested tryptic plasma samples using HILIC-LC-MS/MS, which included mixed human plasma as well as plasma from two healthy individuals collected at three different time points, approximately one month apart. Our focus was on the glycan structure of the Fc domain of IGG subclasses. The results indic...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-06-13 | MSV000095017 | MassIVE
ProteomicsSite-specific analysis of CD16a and CD32a N-glycosylation from monocytes display donor variability which modulate affinity to IgG1 Fc
Glycopeptide mass spectra of CD16a and CD32a from isolated monocytes display donor and site variability. CD16a N-glycosylation composition affects the affinity of IgG1 Fc. Peptide coverage of CD16a was ~85% while CD32a was ~61%.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-06-26 | MSV000084012 | MassIVE
ProteomicsSite-specific glycosylation mapping of Fc gamma receptor IIIb from neutrophils of individual healthy donors
The uploaded dateset corresponds to MS1 and MS2 spectra obtained for Fc gamma receptor IIIb isolated from neutrophils of individual healthy donors. They represent NA1/NA2, NA2/NA2, NA2/NA2 allotype respectively. Based on the data, the targeted analysis of the N-glycosylation has been performed for t...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-08-05 | MSV000085913 | MassIVE
TranscriptomicsHigh titers and low fucosylation of early anti-SARS-CoV-2 IgG promote hyper-inflammation by anti-inflammatory macrophages (MIL10)
Patients diagnosed with coronavirus disease 2019 (COVID-19) mostly become critically ill around the time of activation of the adaptive immune response. Here, we provide evidence that antibodies play a role in the worsening of disease at the time of seroconversion. We show that early phase severe acu...
ORGANISM(S): Homo sapiens 
2021-04-30 | E-MTAB-10431 | biostudies-arrayexpress
ProteomicsFc glycosylation status of Vi vaccine-induced antibodies
Conjugate vaccine against typhoid fever has been shown to be safe and effective in field trials. The mechanism through which the vaccine protects remains elusive. Recent data have implicated antibody glycosylation, and specifically afucosylated antibodies, as an important factor in vaccine-induced e...
ORGANISM(S): Homo sapiens (Human) 
2024-05-30 | PXD037239 | Pride
Immunoglobulin Igg Glycan Vaccine Thyphoid fever 
ProteomicsAntigen-specific IgG Glycosylation Profiles in Hamsters and Macaques Following COVID-19 Vaccination
Vaccination triggers the production of antigen-specific antibodies, including IgG. IgG molecules are glycosylated at the Fc region, and these glycan modifications markedly influence Fc receptor binding and downstream immune functions. Notably, infections with enveloped viruses such as SARS-CoV-2 can...
ORGANISM(S): Mesocricetus auratus (Golden hamster) Macaca mulatta (Rhesus macaque) 
2026-03-11 | PXD068257 | Pride
Glycosylation Antibody Sars-cov-2 Vaccination Covid-19 
ProteomicsEndoglycosidases- treated N-glycosylation site identification
Glycoproteins, representing over 50% of human proteins and most biopharmaceuticals, are crucial for regulating various biological processes. The complexity of multiple glycosylation sites often leads to incomplete sequence coverage and ambiguous glycan modification profiles. Here, we developed an in...
ORGANISM(S): Homo Sapiens 
2024-12-30 | PXD059329 |
ProteomicsDecreased Fc fucosylation aligns with enhanced RSV-specific antibody functionality in adults compared to young children
Respiratory syncytial virus (RSV) is a major cause of severe respiratory tract infections in infants and older adults. While vaccines have recently been approved for older adults and pregnant women, vaccine development for infants remains challenging due to the risk of vaccine-enhanced disease. Unde...
ORGANISM(S): Homo sapiens (Human) 
2025-11-05 | PXD069590 | Pride
Fc-glycosylation Antibody maturation Respiratory virus Fc-functionality 
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