Background
Lead Contributor for Webpage: Carlos Pondevida
Lead Contributor for Webpage: Carlos Pondevida
In simple terms, glycans are an important class of biomolecules that exist as free carbohydrates or in the form of sugar residues attached to a protein (forming a glycoprotein) or lipid (forming a glycolipid). In mammals, about 50% of the proteome are actually glycoproteins and the addition of sugar residues to proteins have a large impact on their function. For instance, the image on the left shows the S protein of the SARS-CoV-2 virus in its native form and what it would look like without glycans.
New methods of detecting glycans are being developed by leveraging the ability of lectins, molecules that bind to them. The need for this stems from issues with the current gold standard practice of using mass spectrometry methods to identify glycans. However, current identification of glycans with mass specs has challenges in that it is costly, requires expert operation knowledge and has low execution speed3. This lends to the need for alternative, easier methods that have a higher ease of operation for research laboratories who are in need of glycoprofiling.
Usage of lectins that can bind glycans is the most promising way to easily identify them. However, with lectin databases being one of the most poorly researched biomolecule profiles, glycan-specific lectin binding profiles databases do not exist. These databases are needed in order to apply recently discovered methods, such as SUGAR-seq4 that utilize lectins to obtain glycoprofiles. Further, the current status of lectin data does not provide much information concerning their self-binding properties since they themselves have glycans. This missing information could obscure their use in glycoprofiling. Analysis of lectin sequencing data can provide intuition to the role of their carbohydrate residues and possibly guide modification of lectins to increase effectiveness.