Modern medicine depends on antibiotics to treat infections by disabling targets inside bacterial cells. Once inside these cells, antibiotics bind to certain sites on specific enzyme targets to stop bacterial growth.
Reviewed by Lily Ramsey, LLMAug 30 2023 Randomly occurring changes in the genes for these targets occur naturally, in some cases making the target harder for the antibiotic to attach to and that bacterial version resistant to treatment.
To address this challenge, a new study led by researchers at NYU Grossman School of Medicine applied a technology called MAGE to generate the full inventory of mutations in the bacterial species Escherichia coli where the antibiotic rifampicin attaches to and disables an essential bacterial enzyme known as RNA polymerase . The study authors created 760 unique RNAP mutants by replacing each of the 38 amino acid building blocks that make up the rifampicin binding site on E.
This work provides a map of antibiotic-bacterial RNAP interactions that will be of value to chemists working to build on the study effects by changing, not bacterial binding site residues, but instead the structure of rifampicin and other antibiotics so that they bind tighter for increased potency.
How rifampicin kills bacteria E. coli stores genetic instructions in DNA chains, but then converts them into a related genetic material in RNA, with RNAP building the RNA chains that guide the building of proteins out of amino acids. The mutants created in the new study revealed that rifampicin kills bacteria by stalling RNAP, and so causing collisions between it and cellular machinery that operates in the same molecular space to duplicate DNA as cells divide and multiply.
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