Disruption of alpha-mannosidase processing induces non-canonical hybrid-type glycosylation |
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| Authors: | Crispin Max Aricescu A Radu Chang Veronica T Jones E Yvonne Stuart David I Dwek Raymond A Davis Simon J Harvey David J |
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| Affiliation: | 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 |
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| Abstract: | ![]()
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. |
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| Keywords: | ADCC, antibody-dependent cell-mediated cytotoxicity CHO, Chinese hamster ovary CID, collision-induced dissociation dHex, deoxyhexose ER, endoplasmic reticulum ESI, electrospray ionization Fuc, fucose Glc, glucose GlcNAc, N-acetylglucosamine GnT, N-acetylglucosaminyltransferase HEK, human embryonic kidney Hex, hexose HexNAc, N-acetylhexosamine Man, mannose MIg, MAM and Ig domains of RPTPμ MS, mass spectrometry NMR, nuclear magnetic resonance PAGE, polyacrylamide gel electrophoresis PBS, phosphate-buffered saline PCR, polymerase chain reaction PNGase F, peptide N-glycosidase F Q, quadrupole RPTPμ receptor protein tyrosine phosphatase-μ s, soluble SDS, sodium dodecyl sulfate Tof, time-of-flight |
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