Discovery of a single-subunit oligosaccharyltransferase that enables glycosylation of full-length IgG antibodies in <i>Escherichia coli</i>.

ABSTRACT: Human immunoglobulin G (IgG) antibodies are one of the most important classes of biotherapeutic agents and undergo glycosylation at the conserved N297 site in the C_H2 domain, which is critical for IgG Fc effector functions and anti-inflammatory activity. Hence, technologies for producing authentically glycosylated IgGs are in high demand. While attempts to engineer Escherichia coli for this purpose have been described, they have met limited success due in part to the lack of available oligosaccharyltransferase (OST) enzymes that can install N-linked glycans within the QYNST sequon of the IgG C_H2 domain. Here, we identified a previously uncharacterized single-subunit OST (ssOST) from the bacterium Desulfovibrio marinus that exhibited greatly relaxe

SUBMITTER: Sotomayor B 

PROVIDER: S-EPMC11580905 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature