New work promises to shed more light on processes whereby bacteria re able to resist drugs and may ultimately contribute towards the search for new treatments for bacterial diseases.
Bacteria contain an enzyme called DNA gyrase. Its job is to coil up (or "supercoil") the DNA of the bacteria. The enzyme works like a tiny machine and during its reaction with the DNA it has to cut the DNA before later sticking it back together again. This is an Achilles heel for the bacteria as cut DNA can be lethal. Indeed, some widely used antibacterial drugs work by stopping gyrase from resealing the DNA. Without coherent DNA, the cells die. Unfortunately bacteria have developed strategies to resist the effects of these drugs. One such strategy involves proteins called pentapeptide repeat proteins (PRPs) which "rescue" DNA gyrase from the drugs. It is important to know how the PRPs do this so that we can design strategies to overcome the resistance. In this, the Bionanoscience and Biochemistry Laboratory, at the Malopolska Centre of Biotechnology, Jagiellonian University, led by Prof. Jonathan Heddle uncovered vital information informing us how PRPs work. The answer is fascinating - the proteins actually seem to mimic the DNA that the enzyme binds to and somehow use this ability to decrease the effectiveness of drugs. As Prof. Heddle points out, “Resistance in bacteria continues to be a major health threat and the more we can understand resistance processes the more we can hope to overcome them.”