The glycome is the entire complement of sugars, whether free or present in more complex molecules, of an organism. An alternative definition is the entirety of carbohydrates in a cell. The glycome may in fact be one of the most complex entities in nature.
Glycosylation, the covalent attachment of sugar moieties (glycans) to proteins, is a significant process in the endoplasmic reticulum and theGolgi apparatus. More than 50% of all proteins within the cell undergo such modification. When bound to proteins, they affect their structure, function, stability, folding, half-life, trafficking, solubility, and their interactions with other proteins.
Glycans vary in terms of glycosylic linkages, position of the hydroxyl group on the anomeric carbon, the number and type of constituent monosaccharides and the degree of branching. Subsequently, their attachment to protein increases the complexity of the proteome.
Based on how glycans are bound to proteins, glycosylation can be classified into
(4) glypiation, and
The HGP is a consortium of research groups with expertise in glycomics that share a common goal of aiming to understand glycan structures and functions in humans. Australia, China, Croatia, Germany, the Netherlands, Singapore, the United Kingdom, and the United States joined the HGP that will support the analysis of glycans in 30,000 human samples by the end of 2021. ECU team joined the HGP as one of the funding members by contributing the personalised medicine perspective via population-based study of variability of the human IgG glycome.
Desired Skills: Qualitative and quantitative statistical analyses
Basic knowledge on Genetics and Epigenetics.
Project Area: Glycosylation; Immunity , Omics
School / Research Centre / Institute: Centre for Precision Health
Project level: Masters, PhD
Funding: Applicant should apply for ECUHDR or RTP Scholarship
Start date: March 2020
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