| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1259649 | Current Opinion in Chemical Biology | 2012 | 7 Pages |
Glycomics and glycoproteomics have become indispensible tools in the study of glycoconjugates. Mass spectrometry based methods are standardly used to study the proteome and/or glycome and these approaches are capable of providing both, qualitative and quantitative information using top down techniques. The human immune system marks a particular area of interest for glycomics and glycoproteomics research since a large number of key proteins in innate and adaptive immunity are glycoproteins. In numerous examples, the crucial influence of glycosylation on critical steps such as receptor interaction and binding has been demonstrated. In this review, we focus on different glycomics and glycoproteomics approaches and their application for studying protein glycosylation in the immune system.
► Glycomics by PGC LC ESI MS enables isobaric glycan separation. ► Modifications in the N-glycans can completely reverse IgG function. ► Glycoproteomics investigates glycan structures in a site-specific manner. ► Glycomics and glycoproteomics are key technologies for probing glycoprotein function. ► Glycan structures on immune cells interact with lectins (C-type lectins, galectins, siglecs, among others).
