Disruption of alpha-mannosidase processing induces non-canonical hybrid-type glycosylation.
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.
Crispin
Max
M
Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Headington, Oxford OX3 7BN, UK. max@strubi.ox.ac.uk
Aricescu
A Radu
AR
Chang
Veronica T
VT
Jones
E Yvonne
EY
Stuart
David I
DI
Dwek
Raymond A
RA
Davis
Simon J
SJ
Harvey
David J
DJ
D000818:Animals; D016466:CHO Cells; D002236:Carbohydrate Conformation; D002460:Cell Line; D006224:Cricetinae; D003412:Cricetulus; D006031:Glycosylation; D006801:Humans; D008358:Mannose / Q000032:analysis / Q000737:chemistry; D011134:Polysaccharides / Q000032:analysis / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D012995:Solubility; D021241:Spectrometry, Mass, Electrospray Ionization; D043323:alpha-Mannosidase / Q000378:metabolism*
D011134:Polysaccharides; D043323:alpha-Mannosidase; D008358:Mannose