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A new study published in the journal Science Advances sheds light on how Gram-negative bacteria like E. coli construct their outer membrane to resemble body armour, which has far-reaching implications for the development of antibiotics.

Magnified view of the E. coli outer membrane showing hexagonal clustering of proteins, alongside body armour for comparison © Dheeraj Prakaash and Syma Khalid

Professor Colin Kleanthous in the Department of Biochemistry at the University of Oxford led the interdisciplinary study, with contributions from colleagues in Oxford and University College London. They undertook a microscopic examination of the outer membrane of E. coli to understand the molecular basis for the protection it affords against many classes of antibiotics. E. coli causes infections such as pneumonia, UTIs and sepsis that are notoriously difficult to treat due to multidrug resistance.

The outer membrane is composed of two types of lipids that stack on top of each other, an unusual arrangement which, it was thought, is solely responsible for making the membrane resistant to antibiotics. As well as lipids, the outer membrane contains numerous proteins which the bacterium relies on to acquire nutrients and excrete waste products. Textbooks classically show these proteins dotted randomly in the membrane, contributing little to its stability or structure.

The discovery of Professor Kleanthous and colleagues came from them asking a simple question: do protein interactions play any role in the structural integrity of the outer membrane?

Read the full story on the University of Oxford website

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