Carbohydrate-Polypeptide Contacts in the Antibody Receptor CD16A Identified through Solution NMR Spectroscopy.

ABSTRACT: Asparagine-linked carbohydrates (N-glycans) are common modifications of eukaryotic proteins that confer multiple properties, including the essential stabilization of therapeutic monoclonal antibodies. Here we present a rapid and efficient strategy for identifying N-glycans that contact polypeptide residues and apply the method to profile the five N-glycans attached to the human antibody receptor CD16A (Fc γ receptor IIIA). Human embryonic kidney 293S cells expressed CD16A with ¹³C_U-labeled N-glycans using standard protein expression techniques and medium supplemented with 3 g/L [¹³C_U]glucose. Anomeric resonances on the protein-linked N-acetylglucosamine residue at the reducing end of the glycan are particularly well suited to studies of multiply

SUBMITTER: Subedi GP 

PROVIDER: S-EPMC5925738 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature