New screening technique paves the way for protein drugs from bacteria

Jun 05, 2013

A cheaper, more efficient technique for developing complex protein drugs from bacteria has been developed at the University of Sheffield.

Using the bacterium E. coli, researchers from the University's Faculty of Engineering showed it was possible to vastly increase the efficiency of the cells producing specifically modified proteins, as well as improve its performance and stability. The modification is present in over two-thirds of human on the market and involves the addition of specific sugar groups to the protein backbone, a process termed glycosylation.

Drugs based on proteins are increasingly important in modern medicine to tackle health problems including diabetes, cancer and arthritis.

Although simple proteins are traditionally made in , these types of complex drugs are made using because they can make human-type glycosylations that will control its efficacy and stability in the body, and avoid immunogenic reactions in patients.

Using bacteria to make proteins for use as medicines could be a more cost effective alternative, since using animal cells is expensive. However, the efficiency of glycoprotein production in is still very poor, with yields often several thousand times lower than in animal cells.

Now, researchers in the Department of Chemical and Biological Engineering at the University of Sheffield, with collaboration from the University of Colorado, are using a technique called inverse , that allows them to screen cells to identify strains that are likely to be the most efficient glycoprotein producers. Using this method, the team were able to produce seven times as much of the protein in laboratory tests.

The team then used to characterise and accurately quantify the proteins being produced by the bacteria. This allowed them to pinpoint modifications that will enable them, ultimately, to improve the performance of the drug.

Professor Phil Wright, who led the research, said: "We believe that this technique will pave the way for pharmacologists to get the same protein yield from bacteria cells as they could from animal cells and also enable them to produce drugs from bacteria that have vastly improved focus and accuracy."

The team also tested the technique on antibody fragments with positive results, showing that their approach could work in different proteins.

Explore further: Canola genome sequence reveals evolutionary 'love triangle'

More information: "Inverse Metabolic Engineering to Improve Escherichia coli as an N-Glycosylation Host", by Jagroop Pandhal, Lauren B. A. Woodruff, Stephen Jaffe, Pratik Desai, Saw Y. Ow, Josselin Noirel, Ryan T. Gill, Phillip C. Wright, is published in Biotechnology and Bioengineering.

Related Stories

New technique for IDing proteins secreted by cells developed

Sep 25, 2012

(Phys.org)—Researchers from North Carolina State University have developed a new technique to identify the proteins secreted by a cell. The new approach should help researchers collect precise data on cell biology, which ...

Test to improve stem cell safety

Jun 04, 2013

CSIRO scientists have developed a test to identify unsafe stem cells. It is the first safety test specifically for human induced pluripotent stem cells (iPS) – as published today in the international journal Stem Cells.

Recommended for you

Canola flowers faster with heat genes

12 hours ago

(Phys.org) —A problem that has puzzled canola breeders for years has been solved by researchers from The University of Western Australia - and the results could provide a vital breakthrough in understanding ...

Sequencing the genome of salamanders

Aug 20, 2014

University of Kentucky biologist Randal Voss is sequencing the genome of salamanders. Though we share many of the same genes, the salamander genome is massive compared to our own, about 10 times as large.

User comments : 0