Challenges of Glycomics


However, when compared with genomics and proteomics, the emerging field of glycomics faces unique and intriguing challenges which derive from the essential aspects of glycan structure–function relationships. While genomics, transcriptomics and proteomics are template-driven processes, the biosynthesis of glycans is a non–template-driven process. Furthermore, deciphering the biochemistry of the interactions between glycans and proteins in the context of a particular biological pathway is complicated by groups of glycan structures making multiple contacts with binding sites on proteins. These issues have made it extremely difficult to develop databases and bioinformatics tools for glycomics.
In spite of the complexities involved, recent technological developments that have been motivated by the need to take an integrated approach to understanding glycan structure–function relationships have advanced the state-of-the-art of glycomics. Supporting this integrated approach are international collaborative efforts including the Consortium for Functional Glycomics (CFG; an international initiative funded by National Institute of General Medical Sciences), Complex Carbohydrate Research Center, EuroCarbDB, and Human Disease Glycomics/Proteome Initiative. These collaborative efforts are developing novel resources and state-of-the-art technologies for advancing this field. Among the goals of these efforts are developing databases and bioinformatics platforms to integrate and disseminate glycomics data to the scientific community.

The formation of these research entities has resulted in rapid growth of innovative contributions to the glycomics field. Key to the success of these global initiatives is the development of bioinformatics databases for storing and disseminating data sets that describe the structure and function of glycans that are readily accessible to researchers across the world via the Internet. This collaboration and integration is critical to research on complex topics of glycan diversity and glycan–protein interactions that are at the core of structure–function relationships of glycans.

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