Disruption of α‐mannosidase processing induces non‐canonical hybrid‐type glycosylation
Crispin M., Aricescu AR., Chang VT., Jones EY., Stuart DI., Dwek RA., Davis SJ., Harvey DJ.
Golgi α‐mannosidase II is essential for the efficient formation of complex‐type glycosylation. Here, we demonstrate that the disruption of Golgi α‐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 ‘Man6‐based’ hybrid‐type glycans reveals a broader in vivo specificity of N‐acetylglucosaminyltransferase I, further defines the arm‐specific tolerance of core α1‐6 fucosyltransferase to terminal α1‐2 mannose residues, and suggests that disruption of Golgi α‐mannosidase II activity is capable of inducing potentially ‘non‐self’ structures.