Q2 · MEDICINE
Article
Author: Maloney, Patrick ; Valente, Elena ; Pinkerton, Anthony B. ; Rahlfs, Stefan ; Simula, Luigi Felice ; Ulliers, Daniela ; Preuss, Janina ; Gosalia, Palak ; Rahbari, Mahsa ; Peddibhotla, Satyamaheshwar ; Berneburg, Isabell ; Jackson, Michael R. ; Buchholz, Kathrin ; Schwarzer, Evelin ; Chung, Thomas D. Y. ; Haeussler, Kristina ; Bode, Lars ; Hershberger, Paul ; Heimsch, Kim C. ; Skorokhod, Oleksii ; Hedrick, Michael P. ; Becker, Katja
In
Plasmodium
, the first two and rate-limiting enzymes of the pentose phosphate pathway, glucose 6-phosphate dehydrogenase (G6PD) and the 6-phosphogluconolactonase, are bifunctionally fused to a unique enzyme named GluPho, differing structurally and mechanistically from the respective human orthologs. Consistent with the enzyme’s essentiality for malaria parasite proliferation and propagation, human G6PD deficiency has immense impact on protection against severe malaria, making
Pf
GluPho an attractive antimalarial drug target.