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The production of therapeutic antibodies to combat pathogens and treat diseases, such as cancer is of great interest for the biotechnology industry. The recent development of plant-based expression systems has demonstrated that plants are well-suited for the production of recombinant monoclonal antibodies with defined glycosylation. Compared to immunoglobulin G (IgG), less effort has been undertaken to express immunoglobulin A (IgA), which is the most prevalent antibody class at mucosal sites and a promising candidate for novel recombinant biopharmaceuticals with enhanced anti-tumor activity. Here, we transiently expressed recombinant human IgA1 against the VP8* rotavirus antigen in glyco-engineered ΔXT/FT  Nicotiana benthamiana  plants. Mass spectrometric analysis of IgA1 glycopeptides revealed the presence of complex biantennary  N -glycans with terminal  N -acetylglucosamine present on the  N -glycosylation site of the CH2 domain in the IgA1 alpha chain. Analysis of the peptide carrying nine potential  O -glycosylation sites in the IgA1 alpha chain hinge region showed the presence of plant-specific modifications including hydroxyproline formation and the attachment of pentoses. By co-expression of enzymes required for initiation and elongation of human  O -glycosylation it was possible to generate disialylated mucin-type core 1  O -glycans on plant-produced IgA1. Our data demonstrate that ΔXT/FT  N. benthamiana  plants can be engineered toward the production of recombinant IgA1 with defined human-type  N - and  O -linked glycans.

Transient Glyco-Engineering to Produce Recombinant IgA1 with Defined N- and O-Glycans in Plants