Research by Prof. Jonathan Heddle from the JU Małopolska Centre of Biotechnology promises to shed more light on processes whereby bacteria are able to resist drugs and may ultimately contribute to the development of new treatments for bacterial diseases. Its results have recently been published in the latest issue of the international journal Nucleic Acids Research.
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 strategies to overcome the resistance can be designed.
Prof. Jonathan Heddle’s team from the Bionanoscience and Biochemistry Laboratory of the Małopolska Centre of Biotechnology at the Jagiellonian University uncovered vital information about 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.”
The full article is available on the Nucleic Acids Research website.
