Bacterial infections caused by Gram-negative bacteria, such as Escherichia coli (E. coli), are a significant challenge to the medical community, especially considering the emergence of new antibiotic resistant bacteria. This study investigates the Pal-TolB protein complex as a new target for antibiotic development against E. coli infections. The Pal-TolB complex plays important roles in maintaining the integrity of E. coli's cell envelope and in the constriction of the outer membrane during cell division. Our study aims to elucidate the molecular details of the Pal-TolB interaction by disrupting Pal-TolB binding using site-directed mutagenesis. We prepared single point mutations in Pal that we hypothesize are in the Pal-TolB binding interface and then tested for changes to Pal-TolB binding using enzyme linked immunosorbent assays (ELISAs). Our preliminary findings suggest that we were able to identify several key residues that dictate the Pal-TolB interaction, which we aim to target with novel antibiotics in the future.
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Gazali et al. (2024) studied this question.
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