Escherichia coli a bacteria considered the food safety bane of restaurateurs, grocers and consumers is a friend. Cornell University biomolecular engineers have learned to use E. coli to produce sugar-modified proteins for making pharmaceuticals cheaper and faster. (Nature Chemical Biology, March 25, 2012.)
Matthew DeLisa, Cornell associate professor of chemical and biomolecular engineering, and his research team, now have published a novel method for engineering human therapeutic glycoproteins simply and quickly by using E. coli bacteria as a platform. Their methods are now being developed and 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. While there are no firm plans yet, the professor hopes that within a year, testing this kind of pharmaceutical could be done at the Weill Cornell Medical College in Manhattan.
Glycoproteins are proteins that are modified at specific amino acid "acceptor" sites with complex carbohydrate structures, or oligosaccharides a basic human chemical reaction that's essential to life. That's why specifically designed, genetically engineered glycoproteins are so commonly used as drugs they bind to certain protein receptor sites and, for example, block cancer cells from multiplying. Among glycoproteins used to treat diseases today are monoclonal antibodies and interferons.
Current manufacturing methods rely mainly on costly, time-consuming mammalian culture cells, such as the Chinese Hamster Ovary (CHO) cell line. The process is also susceptible to viral contamination, further driving up production cost. In fact in 2009, another biopharmaceutical company temporarily shut down its plant after such a contamination occurred.
The Cornell research uses a method to assemble a synthetic pathway for the simple and quick production of a glycoprotein that for
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