New study conducted by scientists shows how MRSA regulates the critical crosslinking of its cell wall in the face of beta-lactam antibiotics.
Modern strains of MRSA have become broadly resistant to antibiotics, including beta-lactam antibiotics, such as penicillins.
In their report, the researchers disclose the discovery of an allosteric domain in the X-ray structure of the penicillin binding protein 2a of MRSA, the enzyme that carries out the crosslinking reaction.
They also documented that the new beta-lactam antibiotic ceftaroline, recently approved by the Food and Drug Administration, is able to bind to the allosteric domain and trigger the same allosteric opening of the active site. This subversion of the allosteric control allows another molecule of ceftaroline to access the active site, which inhibits the function of the enzyme, leading to cell death by MRSA.
The study is published in the Proceedings of the National Academy of Sciences.