Enolase inhibitors as therapeutic leads for Naegleria fowleri infection

(B) The active site of NfENO (PDB 7UGH, grey) overlayed on the human HEX-bound ENO structure (PDB 5IDZ, pink), showing that all residues of the binding pocket are conserved with the sole exception of Lys243, which corresponds to Ser157 in the human enzyme (all other residue numberings refer to NfENO). Carbon atoms of the NfENO 2-phosphoglyceric acid ligand are colored green, while those of HEX are shown in black. The phosphate groups of the two ligands overlap and are both positioned close to NfENO Lys243; the yellow dotted line shows the closest interatomic distance between the Lys243 amine group and the HEX phosphate.
A team of researchers, including Jillian Milanes, Samuel Kwain, Dan Whitehead, and Jim Morris, have published a groundbreaking study in PLOS Pathogens titled “Enolase inhibitors as therapeutic leads for Naegleria fowleri infection.” The study explores the potential of enolase inhibitors, originally developed for treating glioblastoma, as a new approach to combat the life-threatening brain infection caused by the amoeba Naegleria fowleri. Their findings suggest that the inhibitor HEX shows promise in extending survival in animal models, marking a significant step forward in the search for effective treatments against this often fatal condition. Read the article.