Research Fellows Directory
Dr Edward Taylor
University of Lincoln
Bacteriophages are viruses that infect bacteria. They do this by “hijacking” the bacterial metabolism to reproduce. At the end of the life cycle they burst open the bacterial cell to allow the new viral particles out. This is done by a process that involves a “cleaver” enzyme (nature’s catalyst) called a “lysin”. The lysin makes a hole through the bacterial cell wall and, once outside, it binds tightly to specific sugars “signature sugars” on the cell’s surface, this bursts the cell killing it.
The potential impact of our work
Streptococcus pyogenes is an important microbe and responsible for a wide range of diseases. We are working on a bacteriophage which infects S. pyogenes and produces a nasty toxin along with a DNase1 protein, the toxin damages your immune system causing the symptoms of scarlet fever. The Dnase1 protein may enable the bacterium to adopt a more invasive flesh eating form of the infection called Necrotizing fasciitis. Using a technique known as X-ray crystallography we are able to "see" the individual atoms in the protein structures of the bacteriophage proteins. Knowing the position of atoms in the structure, we are able to determine the way the enzyme works and are better placed to stop the action of the DNase1 protein.
Benefits to the wider society
It may be possible to use our work to develop lysins to act against problematic bacteria and use them as antimicrobials. Bacteria such as C. difficile the causative agent of antibiotic-associated diarrhoea and S. mutans a major cause of tooth decay may prove to be excellent targets. The detection of bacteria is both medically and industrially important. We are using parts of the lysin molecule to develop proteins which bind to “signature sugars” on the outside of the bacterial cell. This work may pave the way for a range of smart molecules for the rapid detection of bacteria.
Interests and expertise (Subject groups)