Immunoglobulin A carries sulfated and <i>O</i>-acetylated <i>N</i>-glycans primarily at the tailpiece site - strategies for site-specific <i>N</i>-glycan identification.

ABSTRACT: Sulfated N-glycans from human immunoglobulin A (IgA) were recently discovered via glycomic approaches. However, their site-specific description is still pending. Certain N-glycan structures at specific N-glycosylation sites in IgA are crucial for microbial neutralization and effector functions. For instance, sialylated N-glycans on the C-terminal tailpiece mediate anti-viral activity by interfering with sialic-acid-binding viruses. Sulfated N-glycan epitopes can be ligands for viral proteins and thus play a role in the immune response. In this study, we performed a site-specific screening for sulfated and other rare N-glycans in two commercially available human serum IgA samples employing an in-depth N-glycoproteomic approach, previously dev

SUBMITTER: Zuniga-Banuelos FJ 

PROVIDER: S-EPMC12353717 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature