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Updated: Jul 18, 2026

Production of IgG Fusion Proteins Transiently Expressed in Nicotiana benthamiana
Published on: January 16, 2021
A functional antibody lacking N-linked glycans is efficiently folded, assembled and secreted by tobacco mesophyll
James Nuttall1, Julian K-C Ma, Lorenzo Frigerio
1Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK.
Abstract:
A potential drawback in the use of plants as an expression platform for pharmaceutical proteins such as antibodies is that plant-specific N-glycosylation can result in proteins with altered function and potential antigenicity. In many cases, the N-glycans are essential for the correct folding, assembly and transport of the recombinant proteins. We tested whether progressive removal of glycosylation sites had a detrimental effect on the synthesis, assembly and secretion of a plant-made immunoglobulin G, Guy's 13. Our results indicate that the plant secretory pathway can cope well with aglycosylated antibody chains. The immunoglobulin without N-linked glycans is correctly assembled and secreted by tobacco protoplasts. Capture enzyme-linked immunosorbent assay also shows that antigen-binding properties are unaffected. Our results therefore suggest one possible alternative to the engineering of a humanized glycosylation machinery in plants.
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