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Glycomics and glycoproteomics

Although protein glycosylation is conserved, genome sequence analysis does not reveal the actual glycan composition of a cell or tissue. Cell type, metabolic and developmental states, availability of nutrients and other variables determine the biosynthetic pathway responsible for glycoprotein production. In systems biology, the composition of glycans cannot be predicted and has to be experimentally elucidated.

  • Glycoproteomics is the study of the glycans present in the repertoire of proteins expressed in a given cell, tissue, or organism.
  • Glycoproteomics can also identify when a site is glycosylated (occupancy) and obtain structural and quantitative composition of each glycan.
  • Glycomics studies define the total glycan composition of the system.
  • Because of the complexity and variability in protein glycosylation, glycoproteomics and glycomics approaches are complementary and, when used together, can create a more complete picture of the system.
  • The ultimate goal of glycomics and glycoproteomics is to obtain comparisons between species, developmental states, disease conditions, etc.
  • Interpretation, data analysis, and comparative studies are facilitated by modern bioinformatic tools and databases

References:

Essentials of Glycobiology, 3rd edition. Cold Spring Harbor Laboratory Press; 2015-2017.


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    Publications related to Glycomics and glycoproteomics
  1. Vainauskas, S., Kirk, C.H., Petralia, L., Guthrie, E.P., McLeod, E., Bielik, A., Luebbers, A., Foster, J.M., Hokke, C.H., Rudd, P.M., Shi, X., Taron, C.H 2018. A novel broad specificity fucosidase capable of core a1-6 fucose release from N-glycans labeled with urea-linked fluorescent dyes Sci Rep. , PubMedID: 29934601, DOI: 1038/s41598-018-27797-0
  2. Albrecht, S., Vainauskas, S., Stöckmann, H., McManus, C., Taron, C.H. and Rudd, P.M. 2016. Comprehensive Profiling of Glycosphingolipid Glycans Using a Novel Broad Specificity Endoglycoceramidase in a High-Throughput Workflow. . May 3;88(9), PubMedID: 27033327, DOI:
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