Oral Presentation The 44th Lorne Conference on Protein Structure and Function 2019

Finding the Achilles' Heel in Multi-Drug Resistant Gram-Negative Bacteria (#26)

Tatiana P. Soares da Costa 1 , Chamodi K. Ghardi 1 , Belinda M. Abbott 1 , J. Mark Sutton 2 , Matt Perugini 1
  1. La Trobe University, Bundoora, VIC, Australia
  2. Microbiology Services Division, Public Health England, Salisbury, Wiltshire, UK

The cell wall of Gram-negative bacteria consists of peptidoglycan chains linked together by oligopeptidic sequences comprised of the amino acids L-Ala, D-Ala, D-Glu and meso-diaminopimelate (DAP). Meso-DAP is synthesised via the DAP pathway that also yields the amino acid, L-lysine. Gene knock-out studies show that enzymes functioning in the DAP pathway are essential to bacteria, including dihydrodipicolinate synthase (DHDPS). DHDPS is an allosteric enzyme that catalyses the first-committed and rate-limiting step in DAP biosynthesis. It forms a homo-tetrameric structure that gives rise to at least two ‘druggable’ sites, namely (a) the active site and (b) the allosteric site, which binds lysine to mediate a feedback inhibition response. Given its essentiality to bacteria and absence in humans, DHDPS represents a valid but as yet unchartered target for antibacterial development. Recently, we have developed two classes of small molecule inhibitors that target the DHDPS active site and allosteric site using a contemporary multi-disciplinary workflow spanning biophysics, biochemistry, medicinal chemistry, microbiology and structural biology. Inhibition and binding studies have demonstrated that these compounds are broad-spectrum inhibitors of bacterial DHDPS in vitro, representing the most potent DHDPS inhibitors discovered to date. Using viability and time-kill assays, these inhibitors have been shown to be bactericidal against both drug-sensitive and multidrug-resistant strains of Gram-negative bacteria, including Acinetobacter baumannii, Pseudomonas aeruginosa and Escherichia coli, but are non-toxic to cultured human cells or in vivo to Galleria melanolla at > 20 x Ki. Importantly, these compounds have been shown to inhibit biofilm formation and synergise with FDA-approved classes of antibiotics, including β-lactams, fluoroquinolones, rifampicin and aminoglycosides. This study illustrates the potential for DHDPS inhibitors to be developed into a new class of antibacterials with excellent potential to be combined with current antibiotics to yield innovative multi-targeted formulations to minimise the emergence of resistance.