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DeLisa group paper on bacterial "glycoengineering" featured on the Nature Chemical Biology website

Friday, March 30, 2012

An artificial pathway in E. coli for making glycoproteins

A method for engineering a bacterial strain to create eukaryotic glycoproteins developed by Professor Matthew DeLisa and colleagues is presented this week in Nature Chemical Biology.

These results may have immediate importance for industrial production of glycoproteins that scientists use in looking for therapies for various diseases. Presently, glycoproteins needed for medical treatments and scientific research are created using hard-to-manipulate eukaryotic cells to retain the specific glycans which are critical for biological function: Eukaryotic glycoproteins are labeled with a specific sugar-rich carbohydrate sequence that determines the localization, function, and stability of the corresponding protein. Bacteria also attach carbohydrates to some of their proteins, but the sugar structure is significantly different from the eukaryotic glycoproteins created. DeLisa and colleagues now create an engineered E. coli cell that can produce a five-carbohydrate chain - the ‘core structure’ of the eukaryotic carbohydrate sequence - that can be further attached to several eukaryotic proteins made in the same cell. Their methods are now being commercialized through a startup company, Glycobia Inc., which recently took up residence in Cornell's McGovern Family Center for Venture Development in the Life Sciences:

To read the full article in Nature Chemical Biology:

Various news sources feature the article including;
Eurekalert (AAAS):
Cornell Chronicle:

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