Asymmetric <i>N</i>-Glycosylation in the Tailpiece of Recombinant IgA1.

ABSTRACT: Here, we employed a variety of mass spectrometry (MS)-based approaches, both (glyco)peptide-centric and protein-centric, to resolve the complex glycoproteoform landscape of recombinant IgA1 produced in HEK293 cells. These key immunoglobulins harbor several N- and O-glycosylation sites, making them considerably more heterogeneous than their IgG counterparts. We provide quantitative data on the occupancy and glycan composition for each IgA1 glycosylation site. Combining all data, we revealed that IgA1 molecules consist of at least three distinct populations with varying N-glycosylation site occupancies at the C-terminal tailpiece, namely, one with both glycosylation sites occupied, another with both glycosylation sites unoccupied, and a third asymmetric population with o

SUBMITTER: Peris-Diaz MD 

PROVIDER: S-EPMC11664498 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature