Antibiotic polymyxin arranges lipopolysaccharide into crystalline structures to solidify the bacterial membrane
The uncontrolled rise and spread of Antimicrobial Resistance (AMR) have transformed from individual observations in the 1940–1960s into a worldwide multi-drug resistance (MDR) crisis with a grim projection to kill ~10 million people per year by 2050. Amidst several ongoing innovations to look for solutions, Scientists from Switzerland utilizing new high-resolution microscopic images, showed that Polymyxins, one of the mysterious last-resort antibiotics, crystallize the cell membranes of bacteria. Scientists utilized a powerful tool called atomic force microscopy (AFM) along with structural biology and biochemistry assays to study how polymyxin antibiotics interact with lipopolysaccharide (LPS) in bacterial membranes.
They discovered that polymyxins arrange LPS into hexagonal assemblies to form crystalline structures. After almost a hundred years of its use, scientists provided evidence to suggest that the formation of rigid LPS–polymyxin crystals and subsequent membrane disruption is the mechanism of polymyxin action. This discovery could provide a benchmark for optimization and de novo design of LPS-targeting antimicrobials, with hopes to tackle the AMR problem more efficiently. While these are promising developments for the future, as of now, diagnosing infections promptly using kits like Acutis Reveal™, and treating them appropriately at first is the only measure to curb the burden of AMR.
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