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

ABSTRACT: Although immunoglobulin G (IgG) harbors just one N-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 functionality heavily relies on the precise linkages and branching between monosaccharides, yet these features are challenging to study. Here, by development of a nanohydrophilic interaction chromatography (HILIC)-LC-MS/MS method, we reveal distinct structural glycosylation signatures for each of th

SUBMITTER: Wang W 

PROVIDER: S-EPMC11613209 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature