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Kallolimath, S; Castilho, A; Strasser, R; Grunwald-Gruber, C; Altmann, F; Strubl, S; Galuska, CE; Zlatina, K; Galuska, SP; Werner, S; Thiesler, H; Werneburg, S; Hildebrandt, H; Gerardy-Schahn, R; Steinkellner, H.
(2016): Engineering of complex protein sialylation in plants
P NATL ACAD SCI USA. 2016; 113(34): 9498-9503. FullText FullText_BOKU

Sialic acids (Sias) are abundant terminal modifications of protein-linked glycans. A unique feature of Sia, compared with other monosaccharides, is the formation of linear homo-polymers, with its most complex form polysialic acid (polySia). Sia and polySia mediate diverse biological functions and have great potential for therapeutic use. However, technological hurdles in producing defined protein sialylation due to the enormous structural diversity render their precise investigation a challenge. Here, we describe a plant-based expression platform that enables the controlled in vivo synthesis of sialylated structures with different interlinkages and degree of polymerization (DP). The approach relies on a combination of stably transformed plants with transient expression modules. By the introduction of multigene vectors carrying the human sialylation pathway into glycosylation-destructed mutants, transgenic plants that sialylate glycoproteins in alpha 2,6-or alpha 2,3-linkage were generated. Moreover, by the transient coexpression of human alpha 2,8-polysialyltransferases, polySia structures with a DP >40 were synthesized in these plants. Importantly, plant-derived polySia are functionally active, as demonstrated by a cell-based cytotoxicity assay and inhibition of microglia activation. This pathway engineering approach enables experimental investigations of defined sialylation and facilitates a rational design of glycan structures with optimized biotechnological functions.
Authors BOKU Wien:
Altmann Friedrich
Gr├╝nwald-Gruber Clemens
Kallolimath Somanath
Machado Ferreira Castilho Alexandra
Steinkellner Herta
Strasser Richard

Find related publications in this database (Keywords)
protein polysialylation
Nicotiana benthamiana
recombinant proteins
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