Expression and glycoengineering of functionally active heteromultimeric IgM in plants
Andreas Loosa, Clemens Gruberb, Friedrich Altmannb, Ulrich Mehofera, Frank Henselc, Melanie Granditsd, Chris Oostenbrinkd, Gerhard Stadlmayrb, Paul G. Furtmüllerb, and Herta Steinkellnera,1
Author Affiliations
Edited by Charles J. Arntzen, Arizona State University, Tempe, AZ, and approved February 25, 2014 (received for review November 13, 2013)
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Significance
IgM antibodies are increasingly gaining interest as therapeutics; however, knowledge about this antibody class is scarce. Specifically the impact of N-glycans on the functional mechanism of this heavily glycosylated molecule is entirely unknown. To address this issue we produced different IgM glycoforms in plants and characterized them. Moreover, we present a computer model that explains the characteristic N-glycosylation pattern of IgMs. With the successful in planta generation of recombinant IgMs largely resembling the plasma-derived orthologue, we offer an efficient alternative to mammalian cell-based expression systems. IgMs with targeted glycoengineered N-glycans now enable detailed structure–function studies and will lead to the production of IgMs with optimized in vivo activities.