“What doesn’t kill you, makes you stronger” — this iconic quote of Friedrich Nietzsche applies to bacteria too. When antibiotics cannot kill bacteria, either because of their natural resistance or a patient’s non-adherence to prescriptions, the bacteria develops antibiotic resistance. Antibiotic resistance is one of the biggest crises of public health because if we cannot kill the bacteria, they will end up killing us. The war against antibiotic resistance is on, and in that mission, scientists have made an achievement.
An international team of researchers led by scientists at the Trinity College in Dublin in Ireland have produced a fine blueprint of a bacterial enzyme that “cools down” the immune response of the host during an infection. The enzyme named Lit (lipoprotein intramolecular transacylase) plays a “stealthy” role in developing bacterial infections by mitigating immune responses, found scientists.
The Lit enzyme produces a lipoprotein that engages with the immune response of the host infected by bacteria. “Cooling” down the immune response, the enzyme helps bacteria get a foothold in the infected host. Lipoproteins serve a number of functions in bacterial cells — from keeping them alive to engaging their target’s immune response.
Understanding the structure and functioning of the enzyme at the molecular level can help scientists develop strategies to fight against it. Now that scientists have produced a high-resolution crystal structure and blueprint of the enzyme, they are armed with a detailed understanding of how the enzyme functions. According to scientists, the enzyme is very likely to be a virulence factor — a structure that enables severe infection by a pathogen. The Lit enzyme could be “an important target" for developing critically needed antibiotics, as per Martin Caffrey, the senior author of the study. According to Caffery, “it is no exaggeration to say that antibiotic resistance poses a genuine, growing threat to our society.”
Scientists are also intensely examining other lipoprotein producer and processor enzymes, hoping to find weak targets for antibiotics for which the bacteria could not develop resistance.
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