Featured Research

from universities, journals, and other organizations

E. coli bacteria becomes factory for sugar-modified proteins to make cheaper, faster pharmaceuticals

Date:
March 26, 2012
Source:
Cornell University
Summary:
Escherichia coli – a bacteria considered the food safety bane of restaurateurs, grocers and consumers – is a friend. Biomolecular engineers have learned to use E. coli to produce sugar-modified proteins for making pharmaceuticals cheaper and faster.

The introduction of five specific enzymes into E. coli allows production and transfer of a eukaryotic core structure to several protein targets.
Credit: DeLisa lab

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.

Related Articles


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 forms 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.

The National Institutes of Health, the National Science Foundation, and the New York State Office of Science, Technology and Academic Research funded the work.


Story Source:

The above story is based on materials provided by Cornell University. The original article was written by Anne Ju. Note: Materials may be edited for content and length.


Journal Reference:

  1. Juan D Valderrama-Rincon, Adam C Fisher, Judith H Merritt, Yao-Yun Fan, Craig A Reading, Krishan Chhiba, Christian Heiss, Parastoo Azadi, Markus Aebi, Matthew P DeLisa. An engineered eukaryotic protein glycosylation pathway in Escherichia coli. Nature Chemical Biology, 2012; DOI: 10.1038/nchembio.921

Cite This Page:

Cornell University. "E. coli bacteria becomes factory for sugar-modified proteins to make cheaper, faster pharmaceuticals." ScienceDaily. ScienceDaily, 26 March 2012. <www.sciencedaily.com/releases/2012/03/120326112504.htm>.
Cornell University. (2012, March 26). E. coli bacteria becomes factory for sugar-modified proteins to make cheaper, faster pharmaceuticals. ScienceDaily. Retrieved November 24, 2014 from www.sciencedaily.com/releases/2012/03/120326112504.htm
Cornell University. "E. coli bacteria becomes factory for sugar-modified proteins to make cheaper, faster pharmaceuticals." ScienceDaily. www.sciencedaily.com/releases/2012/03/120326112504.htm (accessed November 24, 2014).

Share This


More From ScienceDaily



More Plants & Animals News

Monday, November 24, 2014

Featured Research

from universities, journals, and other organizations


Featured Videos

from AP, Reuters, AFP, and other news services

Ebola-Hit Sierra Leone's Late Cocoa Leaves Bitter Taste

Ebola-Hit Sierra Leone's Late Cocoa Leaves Bitter Taste

AFP (Nov. 23, 2014) The arable district of Kenema in Sierra Leone -- at the centre of the Ebola outbreak in May -- has been under quarantine for three months as the cocoa harvest comes in. Duration: 01:32 Video provided by AFP
Powered by NewsLook.com
Anglerfish Rarely Seen In Its Habitat Will Haunt You

Anglerfish Rarely Seen In Its Habitat Will Haunt You

Newsy (Nov. 22, 2014) For the first time Monterey Bay Aquarium recorded a video of the elusive, creepy and rarely seen anglerfish. Video provided by Newsy
Powered by NewsLook.com
Birds Around the World Take Flight

Birds Around the World Take Flight

Reuters - Light News Video Online (Nov. 22, 2014) An imperial eagle equipped with a camera spreads its wings over London. It's just one of the many birds making headlines in this week's "animal roundup". Jillian Kitchener reports. Video provided by Reuters
Powered by NewsLook.com
Could Your Genes Be The Reason You're Single?

Could Your Genes Be The Reason You're Single?

Newsy (Nov. 21, 2014) Researchers in Beijing discovered a gene called 5-HTA1, and carriers are reportedly 20 percent more likely to be single. Video provided by Newsy
Powered by NewsLook.com

Search ScienceDaily

Number of stories in archives: 140,361

Find with keyword(s):
Enter a keyword or phrase to search ScienceDaily for related topics and research stories.

Save/Print:
Share:

Breaking News:

Strange & Offbeat Stories


Plants & Animals

Earth & Climate

Fossils & Ruins

In Other News

... from NewsDaily.com

Science News

Health News

Environment News

Technology News



Save/Print:
Share:

Free Subscriptions


Get the latest science news with ScienceDaily's free email newsletters, updated daily and weekly. Or view hourly updated newsfeeds in your RSS reader:

Get Social & Mobile


Keep up to date with the latest news from ScienceDaily via social networks and mobile apps:

Have Feedback?


Tell us what you think of ScienceDaily -- we welcome both positive and negative comments. Have any problems using the site? Questions?
Mobile: iPhone Android Web
Follow: Facebook Twitter Google+
Subscribe: RSS Feeds Email Newsletters
Latest Headlines Health & Medicine Mind & Brain Space & Time Matter & Energy Computers & Math Plants & Animals Earth & Climate Fossils & Ruins