PXD065180

PXD065180 is an original dataset announced via ProteomeXchange.

Title	Raider of the lost N glycans – Localizing rare, easily overlooked IgG N glycans with sulfation or bisecting LacNAc
Description	Immunoglobulin G (IgG) is the most abundant immunoglobulin in human blood. Here it plays a central role in the immune system by recognizing antigens and mediating effector functions of the humoral immune defense. The role of IgG N glycosylation in many of these processes is well known. However, low abundant N glycans with special features, like sulfation or galactosylated bisecting N acetylglucosamine (GlcNAc), are rarely accounted for due to their challenging detection. These structures are frequently overlooked and their presence on IgG is disputed mainly because specialized enrichment and analysis strategies are required for their detection. Consequently, they are disregarded in studies of IgG N glycosylation, which in general is well understood. But functional knowledge is mainly based on N glycans found in IgGs Fc region that contains a conserved N glycosylation site. In contrast, the influence of N glycosylation within the Fab region is less well understood, partly because it is present at non conserved glycosylation sites found on only 10–25% of IgG. Here, we performed an in depth analysis of released N glycans derived from intact IgG, its Fab and its Fc regions. For this we combined proteolytic fragmentation of IgG obtained by affinity chromatography and exoglycosidase sequencing based on multiplexed capillary gel electrophoresis with laser induced fluorescence (xCGE LIF). By using these simple and readily available methods, we localized N glycans bearing sulfation or galactosylated bisecting GlcNAc on IgG, and found them on IgA, too. Further, we proved sulfation of N glycans using an apo sulfatase in an epitope directed glycan enrichment (EDGE )profiling workflow. With our novel findings, we provide insights into hypothetical biological implications of these low abundant N glycan features and advocate for their inclusion in future studies of IgG N glycosylation.
HostingRepository	PRIDE
AnnounceDate	2025-06-19
AnnouncementXML	Submission_2025-06-19_01:10:54.162.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Thilo Kaehne
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; deamidated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2025-06-18 14:55:46	ID requested
⏵ 1	2025-06-19 01:10:54	announced

10.3389/FMOLB.2025.1593708;

submitter keyword: N glycans, IgG

Prof. Dr. Thilo Kaehne
contact affiliation	Institute of Experimental Internal Medicine University Magdeburg Medical School Leipzigerstr. 44 39120 Magdeburg, Germany
contact email	kaehne@med.ovgu.de
lab head
Thilo Kaehne
contact affiliation	University Magdeburg
contact email	kaehne@med.ovgu.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD065180
     1. Label: PRIDE project
     2. Name: Raider of the lost N glycans – Localizing rare, easily overlooked IgG N glycans with sulfation or bisecting LacNAc