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Unusual antibiotics show promise against deadly 'superbugs'

ys research group focused on an enzyme called penicillin-binding protein 2a (PBP 2a), which is unique to MRSA. Research by others showed that the enzyme, located on the bacterial cell membrane, acts as a key defense mechanism by helping the bug maintain a chemical barricade that is impervious to antibiotics.

Mobasherys group recently discovered, in a study published in the Feb. 16 issue of the Journal of the American Chemical Society, that the enzyme interacts with certain components of the bacterial cell wall and that targeting these components might deactivate the enzyme, making the bacteria vulnerable to attack. Subsequently, the group identified a set of three novel cephalosporin antibiotics that appear to interact with the enzyme and also contain protein components that are similar to those of the bacterial cell wall.

The researchers then added the antibiotics to vancomycin-resistant MRSA and compared the results to those of another set of antibiotics belonging to a similar drug class (beta-lactams). The new antibiotics killed the bacteria, whereas the others did not, they say.

Based on lab studies, Mobashery believes that the novel antibiotics gained access to the enzymes active site by mimicking chemical components of the bacterial cell wall, which is largely composed of a polymer called peptidoglycan. Upon contact with the cell wall components, the antibiotics appear to trigger the enzyme to open. Once open, the antibiotics deactivate the enzyme, setting in motion a chain of events that eventually kills the bacteria, the researcher says.

More studies are needed to verify the details of this unique mechanism and to determine whether this mechanism is used by other antibiotics, he adds. So far, only three antibiotics all of them cephalosporin derivatives appear to function by this mimicry mechanism, says Mobashery, whose study was funded by the National Institutes of Health.

Antibiotic resistance is a persiste
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