2024-08-14 08:45:52
The search for new strategies to combat pathogenic bacteria is of global importance.
Bacteria need to adapt to different environments in order to survive and, therefore, they use bacterial receptors in order to adjust their morphology and ensure their survival in changing environments.
A multi-research team from the Zaidín Experimental Station (EEZ, based on the High Commission for Scientific Research (CSIC)), in collaboration with the Crystallographic Research Laboratory of the Andalusian Institute of Earth Sciences (IACT, based on CSIC) and Ohio State University, the latter institution in the United States and the rest in Spain, has identified a large family of bacterial receptors with common characteristics.
In particular, the team led by Elizabet Monteagudo-Cascales from the EEZ has verified that they have the ability to bind to purines, a type of organic material, through a specific pattern conserved in viral proteins. These purines include degradation products of nucleic acids and plant compounds such as caffeine and theophylline. This important advance may open new avenues to the development of methods to combat bacterial infections by interfering with these receptors.
One of the strategies used to fight pathogenic bacteria is that of blocking the signals that cause virulence, that is, preventing the bacteria from executing the processes that allow them to infect and damage the host. This method is based on the activity of the receptors of these bacteria. However, the lack of knowledge about the signals that activate bacterial receptors has made it difficult to develop effective methods to block them and, therefore, prevent virulence. Hence the importance of new training.
Through a combination of structural biology, bioinformatics, protein biochemistry and microbiology techniques, the authors of this study show that the known superfamily includes more than 6,300 receptors spread across many bacterial species, including that is pathogenic for the human body. Likewise, these receptors have important roles in the regulation of gene activity, cellular metabolism, internal signaling and the transport ability of bacteria. The researchers used the bacteria Vibrio cholerae, the causative agent of cholera, as a model in their study, showing that the connection of these receptors to compounds such as theophylline, an abundant purine in tea, increases the levels of the messenger second that controls virulence. .
This work opens up a new way of studying to deal with infectious diseases, interfering with their ability to detect external signals. Likewise, an innovative method to identify and differentiate large groups of viral proteins that bind to compounds called ligands is validated. Furthermore, it was shown that purine derivatives are important external chemical signals that influence bacterial activity, opening new opportunities for the treatment of such infections.
Bacteria on the glass surface. (Photo: EEZ/CSIC)
“The method used in the research is novel and will allow in the future to predict the signals recognized by other families of habitats, which will have a significant impact on the field of microbiology,” points out Tino Krell , EEZ researcher and co-author.
The study is titled “Ubiquitous purine sensor modulates diverse signal transduction pathways in bacteria.” And it was published in the academic journal Nature Communications. (Source: EEZ / CSIC)
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