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An IgE Fab is highlighted (top right), showing Asn-140 and Asn-218 occupied by oligosaccharides in a single orientation. However, in vivo, glycans are very flexible; therefore, the sugar at Asn-168 is represented by a series of plausible conformational overlays to indicate the large surface area of the protein that can be shielded. See Figure 1 for color code. Oligomannose glycans: N-linked glycans that contain from 5–9 mannose residues attached to the chitobiose core 28 and 12% oligomannose glycans.

The yeast glycosylation pathway was modified by the introduction of several human glycosylation enzymes, including mannosidase I and II, N-acetylglucosaminyl transferases I and II, and the uridine 5 -diphosphate (UDP)-N-acetylglucosaminyl transporter. These were successfully localized in the yeast Golgi to generate a synthetic glycosylation pathway that generated glycoproteins with homogeneous N-glycan pools containing the human oligosaccharide GlcNAc2 Man3 GlcNAc2 instead of the oligomannose series (GlcNAc2 Man10−15 ), which is naturally present on the K3 strain of Pichia Pastoris glycoproteins (129).

Crispin MD, Ritchie GE, Critchley AJ, Morgan BP, Wilson IA, et al. 2004. Monoglucosylated glycans in the secreted human complement component C3: implications for protein biosynthesis and structure. FEBS Lett. 566:270–74 64. Wormald MR, Wooten EW, Bazzo R, Edge CJ, Feinstein A, et al. 1991. The conformational effects of N-glycosylation on the tailpiece from serum IgM. Eur. J. Biochem. 198:131–39 65. Baker MD, Wu GE, Toone WM, Murialdo H, Davis AC, Shulman MJ. 1986. A region of the immunoglobulin-mu heavy chain necessary for forming pentameric IgM.

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