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Golgi alpha-mannosidase II is essential for the efficient formation of complex-type glycosylation. Here, we demonstrate that the disruption of Golgi alpha-mannosidase II activity by swainsonine in human embryonic kidney cells is capable of inducing a novel class of hybrid-type glycosylation containing a partially processed mannose moiety. The discovery of 'Man(6)-based' hybrid-type glycans reveals a broader in vivo specificity of N-acetylglucosaminyltransferase I, further defines the arm-specific tolerance of core alpha1-6 fucosyltransferase to terminal alpha1-2 mannose residues, and suggests that disruption of Golgi alpha-mannosidase II activity is capable of inducing potentially 'non-self' structures.

Original publication




Journal article


Febs lett

Publication Date





1963 - 1968


Animals, CHO Cells, Carbohydrate Conformation, Cell Line, Cricetinae, Cricetulus, Glycosylation, Humans, Mannose, Polysaccharides, Protein Processing, Post-Translational, Solubility, Spectrometry, Mass, Electrospray Ionization, alpha-Mannosidase