Researchers have devised a way to attach sugars to proteins using unique biological and chemical methods. This means that large quantities of different glycoproteins can be generated for various medical and biological studies.
When the intestinal bacterium E. coli and the diarrheal pathogen Campylobacter work together, it does not have to result in serious illness. Rather, when biologists and chemists team to use the product of this bacterial collaboration, it opens up a whole new technology with potential pharmaceutical applications. Now, the PhD student Flavio Schwarz from Professor Markus Aebi’s group at the Institute of Microbiology of ETH-Zurich and researchers from the University of Maryland have developed a new method for producing glycoproteins.
E. coli is a well-known biological workhorse that can be used to produce recombinant proteins. The problem is that E. coli is missing many of the functions required to modify proteins with sugar molecules. Markus Aebi’s team, however, recently discovered that Campylobacter can do something that only eukaryotes like human cells can: attach sugar molecules to proteins following synthesis to produce glycoproteins.
The researchers recently reported this ground-breaking work in the journal Nature Chemical Biology. In this engineered glycosylation system, some of the genes from the Campylobacter glycosylation machinery are introduced into E. coli, thereby enabling the E. coli to produce glycoproteins. In a second step, unnecessary parts of the sugars are removed outside the bacterial cells and replaced with chemically synthesized sugar molecules of different size and structure, to produce sugar structures resembling human glycans.