An enolase inhibitor for the targeted treatment of ENO1-deleted cancers

Nat Metab. 2020 Dec;2(12):1413-1426. doi: 10.1038/s42255-020-00313-3. Epub 2020 Nov 23.

Abstract

Inhibiting glycolysis remains an aspirational approach for the treatment of cancer. We have previously identified a subset of cancers harbouring homozygous deletion of the glycolytic enzyme enolase (ENO1) that have exceptional sensitivity to inhibition of its redundant paralogue, ENO2, through a therapeutic strategy known as collateral lethality. Here, we show that a small-molecule enolase inhibitor, POMHEX, can selectively kill ENO1-deleted glioma cells at low-nanomolar concentrations and eradicate intracranial orthotopic ENO1-deleted tumours in mice at doses well-tolerated in non-human primates. Our data provide an in vivo proof of principle of the power of collateral lethality in precision oncology and demonstrate the utility of POMHEX for glycolysis inhibition with potential use across a range of therapeutic settings.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antineoplastic Agents / therapeutic use*
  • Biomarkers, Tumor / genetics*
  • Cell Line, Tumor
  • DNA-Binding Proteins / genetics*
  • Enzyme Inhibitors / therapeutic use*
  • Female
  • Glioma / drug therapy
  • Glycolysis / drug effects
  • Humans
  • Macaca fascicularis
  • Male
  • Mice
  • Mice, SCID
  • Neoplasms / drug therapy*
  • Neoplasms / genetics*
  • Phosphopyruvate Hydratase / antagonists & inhibitors*
  • Phosphopyruvate Hydratase / genetics
  • Precision Medicine
  • Sequence Deletion
  • Structure-Activity Relationship
  • Tumor Suppressor Proteins / genetics*
  • Xenograft Model Antitumor Assays

Substances

  • Antineoplastic Agents
  • Biomarkers, Tumor
  • DNA-Binding Proteins
  • Enzyme Inhibitors
  • Tumor Suppressor Proteins
  • ENO1 protein, human
  • Phosphopyruvate Hydratase