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Researchers make gains in understanding antibiotic resistance

eming paradox, said Steitz, this mutation confers resistance, even though the antibiotic still binds to the mutant ribosome.

The new structural data indicate that the L22 mutation increases the size of a "tunnel" in the ribosome, through which the growing peptide chain moves during synthesis. This tunnel is normally blocked by macrolide antibiotics. In the mutant form, the tunnel widens, which may explain why macrolide antibiotics are no longer effective.

According to Steitz, insights about the ribosomal origins of antibiotic resistance are already being applied to the development of new antibiotics. One company leading the way is Rib-X Pharmaceuticals, which was founded by Steitz and colleagues at Yale. "About half of current antibiotics target the ribosome, and most of them target the large subunit," he said. "So, such advances have the potential for significant clinical impact. The general strategy of Rib-X to overcome resistance is to create new hybrid antibiotics that possess the ability to bind to interact simultaneously with different, nearby sites on the ribosome represented by different classes of antibiotics," he said.

"The idea is to take a bit of one antibiotic and tie it to another. So, if resistance arises due to a mutation in one site, there is still another binding site that can be targeted. It's like multiple drug therapies for HIV, in which the drugs attack several sites at once. And if the virus mutates to avoid the effects of one drug, it still gets hit by another. However, in the case of these antibiotics, the binding sites are linked in one molecule. It's like a multi-drug treatment, but in one compound," he said.


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Source:Howard Hughes Medical Institute


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