Research

Some of the most effective vaccines against bacteria join a glycan from the bacterium’s surface to a carrier protein. These glycoconjugate vaccines protect people of all ages, but they are complex and costly to make by conventional means. We engineer microbes to make them biologically, in a process that can be redesigned quickly, for bacterial diseases of humans and animals. Vaccines prevent infections, so fewer antibiotics are needed, which slows the spread of antimicrobial resistance (AMR). Yet most of the bacteria behind deaths linked to AMR still have no vaccine. New vaccines against them would strengthen the UK’s resilience to AMR.

For example Streptococcal diseases of people and animals, and the bacterium that causes Q fever.

Many protein medicines carry glycans that affect how well they work and how long they last in the body. We are developing bacterial and yeast systems to make these glycoproteins with defined glycans.

We engineer cells to reproduce the glycans that pathogens display, for use in vaccines, in adjuvants (ingredients that strengthen the immune response), and in diagnostic tests.

For example Yeast engineered to display glycans like those of disease-causing fungi.

Bacterial and yeast ‘hosts’, the microbes that do the manufacturing, each have their own glycosylation systems and offer different advantages when we engineer them, so each suits different kinds of glycan. We are developing a range of hosts to draw on those strengths.

For example E. coli, Bacillus and yeast.

Fast screening and detailed structural analysis, shared across sites, test which glycans each engineered cell has made.