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Gewählte Publikation:

Goritzer, K; Goet, I; Duric, S; Maresch, D; Altmann, F; Obinger, C; Strasser, R.
(2020): Efficient N-Glycosylation of the Heavy Chain Tailpiece Promotes the Formation of Plant-Produced Dimeric IgA
FRONT CHEM. 2020; 8, 346 FullText FullText_BOKU

Abstract:
Production of monomeric IgA in mammalian cells and plant expression systems such as Nicotiana benthamiana is well-established and can be achieved by co-expression of the corresponding light and heavy chains. In contrast, the assembly of dimeric IgA requires the additional expression of the joining chain and remains challenging especially in plant-based systems. Here, we examined factors affecting the assembly and expression of HER2 binding dimeric IgA1 and IgA2m(2) variants transiently produced in N. benthamiana. While co-expression of the joining chain resulted in efficient formation of dimeric IgAs in HEK293F cells, a mixture of monomeric, dimeric and tetrameric variants was detected in plants. Mass-spectrometric analysis of site-specific glycosylation revealed that the N-glycan profile differed between monomeric and dimeric IgAs in the plant expression system. Co-expression of a single-subunit oligosaccharyltransferase from the protozoan Leishmania major in N. benthamiana increased the N-glycosylation occupancy at the C-terminal heavy chain tailpiece and changed the ratio of monomeric to dimeric IgAs. Our data demonstrate that N-glycosylation engineering is a suitable strategy to promote the formation of dimeric IgA variants in plants.
Autor*innen der BOKU Wien:
Altmann Friedrich
Duric Stella
Maresch Daniel
Obinger Christian
Strasser Richard
BOKU Gendermonitor:


Find related publications in this database (Keywords)
glyco-engineering
glycosylation
immunoglobulin
monoclonal antibody
recombinant glycoprotein


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