Disruption of alpha-mannosidase processing induces non-canonical hybrid-type glycosylation.

Journal article

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.

Authors: Crispin, M; Aricescu, A; Chang, V; Jones, E; Stuart, D

• Publication status: Published
• Journal: FEBS letters
• Volume: 581
• Issue: 10
• Pages: 1963-1968
• Publication date: 2007-05-01
• DOI: 10.1016/j.febslet.2007.04.020
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: alpha-Mannosidase; CHO Cells; Mannose; Glycosylation; Cell Line; Spectrometry, Mass, Electrospray Ionization; Carbohydrate Conformation; Humans; Protein Processing, Post-Translational; Cricetulus; Solubility; Cricetinae; Animals; Polysaccharides