Ongoing research at the Institute of Food Research, which is strategically funded by BBSRC, is exploring the use of virus-produced proteins that destroy bacterial cells to combat potentially dangerous microbial infections. Bacteriophages produce endolysin proteins that specifically target certain bacteria, and IFR has been studying one that destroys Clostridium difficile, a common and dangerous source of hospital-acquired infections. New research is showing that it is possible to 'tune' these endolysin properties to increase their effectiveness and aid their development as a new weapon in the battle against superbugs.
Clostridium difficile infection (CDI) is a common and growing problem as a cause of infections, especially in hospitals where the characteristics of the bacteria make it difficult to clear. At the moment, antibiotics are used to treat infections, but C. difficile is adept at acquiring resistance, meaning the number of effective antibiotics is ever decreasing.
This has driven the search for new antimicrobials, and at IFR Melinda Mayer and Arjan Narbad have been focussing on bacteriophage endolysins. These are relatively short proteins produced by viruses that specifically target certain species of bacteria and then break open the cell walls. They had previously isolated an endolysin, CD27L, which is active against C. difficile when applied externally, but does not affect a large range of other bacteria. This is important as any potential treatment must not affect the native gut bacteria in patients, whose gut microbiota may already have been disturbed.
However, although CD27L works in the laboratory, its activity would probably not be high enough to cope with the vast numbers of C. difficile cells in a growing population in the harsh gut environment to be used as an effective treatment. This prompted the researchers to look more closely at the endolysin.
Endolysins commonly have two domains, on
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| Contact: Andrew Chapple andrew.chapple@nbi.ac.uk 01-603-251-490 Norwich BioScience Institutes Source:Eurekalert |
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