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We demonstrated that our synthetic substrate could be used as a sensor for LytM cat185–316 activity, but we wanted to see whether it could be turned “on” by other muralytic enzymes in cellular environments. To this end, we compared the activity of LytM cat185–316 against the catalytic domain of lysostaphin (LSS cat251–384 ). Lysostaphin is a glycyl-glycine hydrolase that is effective at killing MRSA.
Abstract Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, remains the deadliest human pathogen. Treatment is hampered by drug resistance and the persistence of slow-growing or non-replicating populations. Rifampicin, a cornerstone of first-line therapy, inhibits transcription during promoter escape, but resistance mutations undermine efficacy and drive resistance spread.
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