Glycosylation is the most abundant modification of proteins, variations of which occur in all living cells. Glycosylation can be further categorized into N-linked (where the oligosaccharide is conjugated to Asparagine residues) and O-linked glycosylation (where the oligosaccharide is conjugated to Serine, Threonine and possibly Tyrosine residues). Within the family of O-linked glycosylation, the oligosaccharides attached can be further categorized according to their reducing end residue: GalNAc (often described as mucin-type, due to the abundance of this type of glycosylation on mucins), Mannose and Fucose. This section reviews currently known congenital disorders of glycosylation associated with defects of protein O-glycosylation (Cylwik et al. 2013, Freeze et al. 2014).
Chong, JX, Bamshad, MJ, Freeze, HH, Ng, BG
Chrostek, L, Lipartowska, K, Cylwik, B, Gruszewska, E
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