Saldova Radka, Stöckmann Henning, O'Flaherty Roisin, Lefeber Dirk J, Jaeken Jaak, Rudd Pauline M
NIBRT GlycoScience Group, National Institute for Bioprocessing Research and Training , Fosters Avenue, Mount Merrion, Blackrock, Dublin 4, Ireland.
Department of Neurology, Translational Metabolic Laboratory, Radboud University Medical Centre , Nijmegen, The Netherlands.
J Proteome Res. 2015 Oct 2;14(10):4402-12. doi: 10.1021/acs.jproteome.5b00709. Epub 2015 Sep 24.
MAN1B1-CDG has recently been characterized as a type II congenital disorder of glycosylation (CDG), disrupting not only protein N-glycosylation but also general Golgi morphology. Using our high-throughput, quantitative ultra-performance liquid chromatography assay, we achieved a detailed characterization of the glycosylation changes in both total serum glycoproteins and isolated serum IgG from ten previously reported MAN1B1-CDG patients. We have identified and quantified novel hybrid high-mannosylated MAN1B1-CDG-specific IgG glycans and found an increase of sialyl Lewis x (sLex) glycans on serum proteins of all patients. This increase in sLex has not been previously reported in any CDG. These findings may provide insight into the pathophysiology of this CDG.
最近，MAN1B1-CDG被认定为II型先天性糖基化障碍（CDG），它不仅会破坏蛋白质N-糖基化，还会影响高尔基体的整体形态。通过我们的高通量定量超高效液相色谱分析方法，我们对10名先前报道的MAN1B1-CDG患者的总血清糖蛋白和分离出的血清IgG中的糖基化变化进行了详细表征。我们鉴定并定量了新型杂合高甘露糖基化的MAN1B1-CDG特异性IgG聚糖，并发现所有患者血清蛋白上的唾液酸化路易斯x（sLex）聚糖有所增加。此前在任何CDG中均未报道过sLex的这种增加情况。这些发现可能有助于深入了解这种CDG的病理生理学。
