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From scourge to saint: E. coli bacteria becomes a factory - to make cheaper, faster pharmaceuticals
Date:3/26/2012

ms the basis of many of today's therapeutic protein drugs, including, for example, the protein GCase, used in a drug that treats Gaucher's disease. To do so, they artificially introduced the machinery of glycosylation the chemical process by which proteins become glycoproteins into E. coli cells, rather than animal cells.

The synthetic pathway they designed, which can be tailored to many amino acid acceptor sites to make different drugs, starts with native enzymes in E. coli. Added to that was a mixture of four enzymes taken from yeast cells, which triggered the biosynthesis of a specific glycan (sugar structure) that resembles the core structure found in virtually all eukaryotic glycans. A fifth enzyme from the bacterium, Campylobacter jejuni, transferred these core glycans to pre-engineered protein acceptor sites, resulting in the desired glycoproteins.

DeLisa and his colleagues are now working to improve their approach that they call "glycans by design" using the enzyme-based protein production method to specifically tailor sugar structures to make many different glycans and glycoproteins.


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Contact: Blaine Friedlander
bpf2@cornell.edu
607-254-8093
Cornell University
Source:Eurekalert

Page: 1 2

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