Interestingly, the binding interaction is distinct from other known inhibitors of translation, suggesting it may find use when those agents are not effective. Using cryo-electron microscopy, the authors showed that streptothricin-F bound extensively to a subunit of the bacterial ribosome, accounting for the translation errors these antibiotics are known to induce in their target bacteria. Both were highly selective for Gram-negative bacteria. The D form was more powerful than the F form against drug-resistant Enterobacterales and other bacterial species but caused renal toxicity at a lower dose. Here, the authors characterized the antibacterial action, renal toxicity, and mechanism of action of highly purified forms of two different streptothricins, D and F. More recent work has shown that the multiple forms have different toxicities with one, streptothricin-F, significantly less toxic, while remaining highly active against contemporary multidrug-resistant pathogens. However, the rise of antibiotic-resistant bacterial infections has spurred the search for new antibiotics, leading Kirby and colleagues to take another look at nourseothricin.Įarly studies of nourseothricin suffered from incomplete purification of the streptothricins. But nourseothricin proved toxic to kidneys, and its development was dropped. Its discovery in the 1940s generated high hopes for it as a powerful agent against Gram -negative bacteria, which, due to their thick outer protective layer, are especially hard to kill with other antibiotics. Nourseothricin is a natural product made by a soil fungus, which contains multiple forms of a complex molecule called streptothricin. The findings by James Kirby, MD, of Harvard Medical School and colleagues may offer a new way to fight difficult-to-treat and potentially lethal infections. A neglected 80-year-old antibiotic may provide much-needed protection against multidrug-resistant bacterial infections, according to a new study published in PLOS Biology.
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