Publications by authors named "Zuzanna Pakosz"

Antibiotic metabolites and antimicrobial peptides mediate competition between bacterial species. Many of them hijack inner and outer membrane proteins to enter cells. Sensitivity of enteric bacteria to multiple peptide antibiotics is controlled by the single inner membrane protein SbmA.

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Malaria persists as a major health problem due to the spread of drug resistance and the lack of effective vaccines. DNA gyrase is a well-validated and extremely effective therapeutic target in bacteria, and it is also known to be present in the apicoplast of malarial species, including Plasmodium falciparum. This raises the possibility that it could be a useful target for novel antimalarials.

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Article Synopsis
  • - DNA gyrase is a bacterial enzyme that is targeted by natural toxins and synthetic drugs, like fluoroquinolones, but resistance can occur through proteins known as pentapeptide repeat proteins (PRPs).
  • - The study reveals that a specific PRP, QnrB1, protects against fluoroquinolones by interacting with the GyrB protein and enhancing its ATP hydrolysis activity.
  • - Researchers identified the binding site of QnrB1 on GyrB and suggest that its binding helps release fluoroquinolones from their action site, thereby contributing to antibiotic resistance.
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