Glycans processing

Fig. 15.3 Plant and mammalian N-glycans have different structures. As illustrated here, a core structure (in gray) is common to plant and mammalian biantennary complex N-glycans. However, differences in the glycan processing machineries in plants and in mammals result in the absence of sialic acids in the terminal position of the antennae and the presence of a bisecting p (1,2) -xylose and of an a(l,3)-fucose residue in PMPs instead of the a(l,6)-fucose linked to the proximal N-acetylglucos-amine of native mammalian N-glycans.

Chen, M., Liu, X., Wang, Z., Qi, Q., and Wang, P.G. 2005. Modification of plant V-glycan processing the future of producing therapeutic protein by transgenic plants. Medical Research Reviews 25(3), 343-360. 

K. Karaveg, A. Siriwardena, W. Tempel, Z.-J. Liu, J. Glushka, B.-C. Wang, and K. W. Moremen, Mechanism of class 1 (glycosylhydrolase family 47) a-mannosidases involved in iV-glycan processing and endoplasmatic reticulum quality control,./. Biol. Chem., 280 (2005) 16197-16207. 

F. Vallee, K. Karaveg, A. Herscovics, K. W. Moremen, and P. L. Howell, Structural basis for catalysis and inhibition of /V-glycan processing class I a-l,2-mannosidases, J. Biol. Chem., 275 (2000) 41287-41298. 

Fig. 21. Photograph of the SweetBlot machine, an automated glycan-processing system based on the glycoblotting method. This prototype machine is the latest version, designed for eventual combination with MALDI-TOFMS.

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