Oral Presentation 25th International Pathogenic Neisseria Conference 2026

Investigating the R‑loop resolving enzyme RNase HI as a novel drug target in Neisseria gonorrhoeae (140564)

Kate Pennycuick 1 2 , Joanna Hicks 2 3 , Andrew Thompson 1 2 , Stephanie Dawes 1 2 , J. Shaun Lott 1 2
  1. University of Auckland, Auckland, New Zealand
  2. Maurice Wilkins Centre for Molecular Biodiscovery, Auckland, New Zealand
  3. University of Waikato, Hamilton, New Zealand

The relentless rise of antibiotic-resistant strains of Neisseria gonorrhoeae threatens our ability to effectively treat gonorrhoea, posing a critical threat to public health. The rapid development of resistance underscores the urgent need for new antibiotics with novel mechanisms of action. RNase HI degrades the RNA strand of RNA:DNA hybrids to resolve transcription‑associated R‑loops and is genetically essential in N. gonorrhoeae, representing an unexploited vulnerability1.

Our work validates RNase HI as a potential drug target in N. gonorrhoeae by identifying novel RNase HI inhibitors through a multidisciplinary approach including enzyme activity and bacterial cell viability assays. A chemical scaffold library was synthesised, incorporating a canonical metal-chelating motif tailored to the enzyme's active site, as well as including FDA-approved antivirals originally designed against RNase H-like viral enzymes. A FRET enzymatic assay enabled screening of compound potency against purified N. gonorrhoeae RNase HI, allowing inhibitors to be identified. A bacterial viability assay was then used to determine the antibacterial efficacy of these compounds, with several emerging as dual-activity hits, inhibiting RNase HI catalysis and reducing N. gonorrhoeae viability at low micromolar concentrations. To confirm the specificity of these hits, compounds were then counter-screened against human RNase H1 to ensure limited off-target toxicity. Structure-activity relationships from this biochemical and microbiological data guide iterative optimisation. We have determined the N. gonorrhoeae RNase HI structure at 1.5 Å resolution using X-ray crystallography, and crystal-soaking experiments have yielded inhibitor-bound complexes, providing a framework for improving compound affinity through structural-based drug design.

Our integrated biochemical, microbiological, and structural approach has validated RNase HI as a novel, druggable, pathogen‑selective target. This work paves the way to advancing next‑generation N. gonorrhoeae therapeutics capable of overcoming existing resistance mechanisms.

 

  1. Prister, L. L., Ozer, E. A., Cahoon, L. A., & Seifert, H. S. (2019). Mol. Microbiol. 122, 4. 1219-1234.