Abstract
Glycosylation is the most common posttranslational modification of proteins and plays diverse roles in numerous biological processes, including fertilization, development, differentiation, inflammation, cancer metastasis, and host–pathogen/parasite interactions. A number of glycosylated proteins are bioactive molecules of medical/therapeutic or other commercial interest and are currently produced by recombinantly transformed cells and organisms. Among non-animal expression systems, plant cells and transgenic plants are considered an attractive alternative system for recombinant human and animal glycoproteins. The advantages of using plants for the production of commercially important glycosylated proteins include lower manufacturing costs and a reduced risk of transmitting mammalian pathogens [11, 27]. However, a major roadblock in the use of plants for this purpose is the lack of available information on N- and O-linked glycans in plants and specifically those in the endogenous plant glycosylation pathways [9, 31]. Thus, gathering detailed structural information on plant-derived glycoproteins is of utmost importance.
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Acknowledgements
Lokesh Joshi and Jared Q. Gerlach would like to thank Professors Hans-Joachim Gabius and Harold Rudiger for their helpful discussions. The authors would like to acknowledge the Wallace Research Foundation and the Biodesign Institute at Arizona State University for their financial support.
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Gerlach, J.Q., Kilcoyne, M., Eaton, S., Bhavanandan, V., Joshi, L. (2011). Non-carbohydrate-Mediated Interaction of Lectins with Plant Proteins. In: Wu, A. (eds) The Molecular Immunology of Complex Carbohydrates-3. Advances in Experimental Medicine and Biology, vol 705. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-7877-6_12
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