Improving the N-glycosylation occupancy of plant-produced IgG1 by engineering the amino acid environment at Asn297.

ABSTRACT: Monoclonal antibodies are crucial recombinant biopharmaceuticals, with N-glycosylation at Asn297 essential for their functionality. Plants are increasingly used for antibody production, achieving high expression levels and enabling glycoengineering to produce homogenous human-like N-glycan structures. However, plant-produced human IgG1 often shows significant underglycosylation with potential adverse effects for immune functions and stability. This study addressed this limitation of the widely used plant-based expression platform Nicotiana benthamiana by employing protein engineering to enhance N-glycosylation occupancy in plant-produced IgG1. This was achieved through an amino acid mutation near the conserved glycosylation site in the CH2 domain of the heavy ch

SUBMITTER: Goritzer K 

PROVIDER: S-EPMC11794253 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature