These films form around foreign materials in the body—such as a catheter—and cannot be defeated by conventional means. Researchers say this protein pair could prove to be an important target for developing new antibiotics to fight infections.
In a paper published this week in the Journal of Biological Chemistry, researchers describe a couple of prime suspect genes and the “toxin-antitoxin” protein pair they produce.
By analyzing the structure and binding of the proteins in the exquisite detail of atomic-scale X-ray crystallography, the team at Brown University and Texas A&M University makes the case that “MqsR” and “MqsA” proteins are important operators worth targeting in hopes of disrupting the formation of biofilms.
“Developing new antibiotics has been very difficult, and they all pretty much target the same few proteins,” says corresponding author Rebecca Page, assistant professor of molecular biology, cell biology and biochemistry at Brown. “Our proteins belong to a family of proteins that have never been investigated for their ability to lead to novel sets of antibiotics. This really provides a new avenue.”
The main role of the combination, or complex, of MqsA and MqsR is that they appear to control the transcription of many genes, including ones that govern the growth of “persister” cells, which provide biofilms with a mesh of antibiotic-resistant constituents. In normal populations, persisters are one in a million. In biofilms, they are one in a hundred.
