NIH to fund glycomics center at Emory

The National Center for Functional Glycomics will be funded by a five-year award from the National Institute of General Medicines worth more than $5.5 million

Kelsey Kaustinen
ATLANTA—The National Institutes of Health (NIH) haveannounced plans to fund a new National Center for Functional Glycomics (NCFG),which will be housed at the Emory University School of Medicine. The new centerwill be funded by a five-year award from the National Institute of GeneralMedical Sciences (NIGMS) worth more than $5.5 million, which can potentially berenewed every five years.
 
 
The NCFG will be directed by Richard D. Cummings, Ph.D.,William Patterson Timmie Professor and chair of the Department of Biochemistryat Emory. Cummings also serves as the leader of the Consortium for FunctionalGlycomics, another program from the NIH/NIGMS and the world's largest group ofglycoscientists and biomedical researchers in the field of glycomics.
 
"Emory's Glycomics Center is pleased to lead this effort inadvancing the fields of glycobiology and glycomics, which are increasinglyrecognized as being of critical importance to advances in biomedical researchand treatment of disease," said Cummings in a press release. "Our future plansare to build on the technological breakthroughs in glycomics over the pastdecade and develop new tools for exploring the rich biological roles of glycansin disease and health."
 
 
In addition to Cummings, who will serve as principalinvestigator, personnel for the NCFG also include David F. Smith, Ph.D.,technical director and professor of biochemistry; Tongzhong Ju, M.D., Ph.D.,project leader and associate professor of biochemistry; Xuezheng Song, Ph.D.,project leader and assistant professor of biochemistry; and JamieHeimburg-Molinaro, Ph.D., project coordinator.
 
This grant from the NIH will be used to fund research intothe recognition of glycans and complex carbohydrates through the use of "glycanmicroarrays," platforms that contain microscopic outlays of diverse glycansthat might be recognized by antibodies, proteins, viruses and bacteria. Inaddition to this work, the NCFG will specifically focus on developingtechnology for the glycosciences, particularly to aid in exploring themolecular mechanisms of glycan recognition by proteins within the body thatplay roles in human biology and disease.
 
Glycans are polysaccharides or oligosaccharides, and theglycans found on glycoproteins and glycolipids and in body fluids represent theglycome, which is similar to the genome and the proteome. Changes inglycosylation—the process in which glycans are attached to proteins, lipids orother molecules—play a role in numerous diseases and conditions, such ascancer, cystic fibrosis, inflammation and congenital disorders ofglycosylation. Glycans on human cells are bound by viruses and bacteria thatconsist of the frontrunners in invasion and infection.
 
 
SOURCE: Emory University press release


Kelsey Kaustinen

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