Proteomics

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Human IgG subclasses differ in structural elements of their N-glycosylation

ABSTRACT: 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 indicated that each IGG subclass possesses a distinct glycan signature. Although there were slight variations between individuals, the glycan signature of IGG subclasses in individual plasma remained stable over time.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Karli Reiding  

PROVIDER: MSV000095017 | MassIVE | Thu Jun 13 01:59:00 BST 2024

REPOSITORIES: MassIVE

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Publications

Human IgG Subclasses Differ in the Structural Elements of Their <i>N</i>-Glycosylation.

Wang Weiwei W   Maliepaard Joshua C L JCL   Damelang Timon T   Vidarsson Gestur G   Heck Albert J R AJR   Reiding Karli R KR  

ACS central science 20241010 11

Although immunoglobulin G (IgG) harbors just one <i>N</i>-glycosylation site per heavy chain, this glycosylation plays a key role in modulating its function. In human serum, IgG is classified into four subclasses (IgG1, IgG2, IgG3, IgG4), each characterized by unique features in their sequences, disulfide bridges and glycosylation signatures. While protein glycosylation is typically studied at the compositional level, this severely underestimates the complexity of the molecules involved. Glycan  ...[more]