Abstract
Glyco-bioinformatics means different things to different people. It ranges, for example, from the mining of the genome for glycosylation pathway enzymes, through to analysis of microarray expression of glycosyltransferases, to glycoprotein identification data, to the development of tools that facilitate the interpretation of mass spectra and to the construction of structural glycan databases. Lastly, these data need to be mined so that the function of the glycan structures attached to the range of glycoconjugates in nature can be determined. The quality of the data in these databases needs to be maintained for this work to be meaningful.For easier analysis, glycan structures are often characterised independent of the protein on which these sugars were originally attached. GlycosuiteDB ("http://glycosuitedb.expasy.org/glycosuite/glycodb":http://glycosuitedb.expasy.org/glycosuite/glycodb) is a freely accessible resource that has annotated this glycan structural data with protein and tissue information that sets the basis of functional interpretation. Information on cellular interactions associated with changes in glycosylation structures is essential for the understanding of the functional role of sugars and needs to be collected in order to exploit the knowledge of these posttranslational additions to proteins. One such database is SugarBind ("http://sugarbind.expasy.org/sugarbind":http://sugarbind.expasy.org/sugarbind), which collates the known glycan binding sites of human pathogens. These structural glycan epitopes occur on both proteins and lipids and will add to the knowledgebase of glycosylation function and expand the structural data contained in GlycoSuiteDB. In this presentation, the knowledge obtained on the function of glycosylation by linking the information between two databases will be highlighted as an example of the value to be gained from manual curation of literature-extracted knowledge.
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Lisacek, F. Functional annotation of bacterial sugars. Nat Prec (2010). https://doi.org/10.1038/npre.2010.5107.1
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DOI: https://doi.org/10.1038/npre.2010.5107.1