Congratulations to Prof. Xiulian Yu and collaborators, including Prof. Tao Ni from The University of Hong Kong and Prof. Robert J. C. Gilbert from the University of Oxford, on revealing the molecular mechanism of pore formation by Plasmodium Perforin-like Protein 2, as reported in Nature Communications:
https://doi.org/10.1038/s41467-026-76236-6
Malaria remains one of the world’s most devastating parasitic diseases, causing over 200 million cases each year. With the growing challenges of antimalarial drug resistance and vector control, understanding the molecular mechanisms underlying Plasmodium infection and transmission is critical for developing novel therapeutic intervention. Throughout their complex life cycle, Plasmodium parasites must cross and breach diverse host cells. While perforin-like pore-forming proteins play important roles in these processes, the molecular mechanism of their assembly and pore formation have remained poorly understood.
In this international collaborative study, the team utilized cryo-electron microscopy (SPA and cryo-ET) to reveal how Plasmodium Perforin-like Protein 2 (PLP2) perforates red blood cell membranes, enabling the parasite to escape. These findings resolve a pivotal step in the malaria parasites life cycle and establish a structural blueprint for developing potential transmission-blocking antimalarials.
This work has also been reported on MalariaWorld:
