es is more difficult, compared with proteins or DNA, because glycans form branched structures in which not every link is chemically the same. Scientists have estimated that cells contain hundreds or thousands of different glycans, which can be attached to proteins or lipids. When using the shotgun approach, if scientists find that proteins from the body -- antibodies or toxins, for example -- bind to one particular glycan spot, they can then go back to that spot and determine its entire sequence, sifting out important glycans from the thousands on the slide.
"The sugars present on glycoproteins and glycolipids can contribute decisively to these molecules' functions," says Pamela Marino, PhD, who oversees glycobiology grants at the National Institutes of Health's National Institute of General Medical Sciences (NIGMS). "Understanding what information is encoded in these sugars and how they facilitate interactions with other proteins has been a major road block in deciphering the molecular language of glycans. This study, which is funded through the NIGMS EUREKA program for high risk research, has now provided proof of principle for an extremely novel 'shotgun' approach to interpreting this glycan code, and allows for examination of the role of glycans in infection and immunity."
The Emory team applied shotgun glycomics to red blood cells, tumor cells and brain-derived lipids. Cummings says the technique could be used to look for distinct sugar molecules displayed by cancer cells, for example. Identifying cancer-specific glycans could similarly lead to diagnostic tools or therapies, he says.
"A slide displaying glycans from a given cell type can be thought of as a book in the library, with the entire library constituting the human glycome," he says.
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