Publications by authors named "A D Baughn"
Pyrazinamide (PZA) is a critical component of tuberculosis first-line therapy due to its ability to kill both growing and non-replicating drug-tolerant populations of within the host. Recent evidence indicates that PZA acts through disruption of coenzyme A synthesis under conditions that promote cellular stress. In contrast to its bactericidal action , PZA shows weak bacteriostatic activity against in axenic culture.
View Article and Find Full Text PDFposes a serious challenge for human health, and new antibiotics with novel targets are needed. Here we demonstrate that an acylaminooxadiazole, MBX-4132, specifically inhibits the -translation ribosome rescue pathway to kill . Our data demonstrate that MBX-4132 is bactericidal against multiple pathogenic mycobacterial species and kills in macrophages.
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- Pyrazinamide (PZA) is crucial in treating tuberculosis, specifically targeting non-growing bacteria by disrupting coenzyme A synthesis, but its effectiveness can be hampered by drug resistance.
- A new analog called morphazinamide (MZA) has been studied, showing that it also disrupts coenzyme A synthesis but doesn't need the same environmental stressors as PZA.
- MZA demonstrates a dual action mechanism, allowing it to kill bacteria faster and withstand resistance, offering valuable insights for developing better tuberculosis treatments.
Article Synopsis
- MAH (Mycobacterium avium subsp. hominissuis) is a common mycobacterium causing infections in humans and animals, particularly linked to outbreaks in pigs.
- The study analyzed 50 MAH isolates from pigs in Japan, revealing a genetic connection between these isolates and those found in humans from North America, Europe, and Russia, but not in East Asia.
- Researchers identified a new lineage of MAH (SC5) and emphasized that pig farms are influenced by environmental strains and human infections, highlighting two main transmission routes: environmental exposure and pig movement.
PLP-dependent enzymes represent an important class of highly "druggable" enzymes that perform a wide array of critical reactions to support all organisms. Inhibition of individual members of this family of enzymes has been validated as a therapeutic target for pathologies ranging from infection with Mycobacterium tuberculosis to epilepsy. Given the broad nature of the activities within this family of enzymes, we envisioned a universally acting probe to characterize existing and putative members of the family that also includes the necessary chemical moieties to enable activity-based protein profiling experiments.
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