Last Updated: 02/10/2025
Structural analysis of the Plasmodium V-ATPase bound to candidate antimalarial drugs
Objectives
The main aim of this study is to resolve the atomic structure of Plasmodium V-ATPase bound to candidate antimalarial drugs using cryo-electron microscopy, thereby guiding the design of safer and more effective antimalarial therapies.
Malaria, a disease caused by infection of red blood cells by single-celled Plasmodium parasites, imposes a significant health burden around the world. Over half the world’s population is exposed to malaria, causing 241 million cases and 627,000 deaths in 2020 alone. These malaria infections are increasingly drug resistant, so discovery of new malaria treatments is needed. Plasmodium parasites possess an important molecule called the V-ATPase. The V-ATPase is responsible for controlling the acidity of different parts of the Plasmodium cell and helps the parasite acidify the red blood cell it infects. Recent experiments identified the Plasmodium V-ATPase as a target for antimalarial molecules because blocking the V-ATPase results in Plasmodium cell death. The researcher will determine the atomic structure of the Plasmodium V-ATPase bound to new antimalarial drugs. An approach called electron cryomicroscopy will be used to reveal the positions of all the atoms in the V-ATPase and the bound drug candidates. Determining the high-resolution structure of the Plasmodium V-ATPase bound to candidate antimalarial drugs will guide the iterative design and development of safer, more effective antimalarials, helping to reduce the global health burden of malaria.
Sep 2023 — Aug 2024
$12,828
Related Resources
