Bacterial enzyme switch could weaken antibiotic defenses in MRSA and other pathogens
If you ask Vijay Parashar, associate professor of medical and molecular sciences (MMSC) at the University of Delaware College of Health Sciences, human bodies are bags of bacteria. "It sounds gross, but not all bacteria are bad; most of them are good. The trouble starts when the bad bacteria learn how to outsmart antibiotics."
A groundbreaking study led by the University of Delaware has identified a molecular switch within a bacterial enzyme that could weaken antibiotic defenses in dangerous pathogens like MRSA. Professor Vijay Parashar's team discovered how this enzyme, GdpP, changes shape to regulate the production of c-di-AMP, a chemical messenger crucial for bacterial survival under stress or when exposed to antibiotics.
By capturing the enzyme in multiple structural states using cryo-EM technology, the researchers have uncovered a key point where the bacterial stress response can be disrupted. This insight could lead to new drugs that block GdpP, forcing bacteria into a 'permanent panic' and making existing antibiotics more effective. The discovery, published in the journal Structure, marks a significant step forward in combating antibiotic resistance, potentially paving the way for companion drugs to enhance the potency of current antibiotics.
The research also highlights the broader applications of this structural biology work, including cancer immunotherapy, demonstrating the interdisciplinary nature of scientific advancements.
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