疟原虫致病的机制是什么？ z-bo 2020-10-16 326

　　Recently, the "eLife" magazine published new insights into the molecular mechanisms that allow Plasmodium to spread and spread the disease to its host. The movement and infectivity of the parasite Plasmodium falciparum, and the ability to eventually spread malaria in humans, depend on A polymer compound called a glider. These new discoveries provide a blueprint for future anti-malaria treatment design for anti-slip body movement and its regulating elements.

　　Plasmodium, including the most serious Plasmodium falciparum, causes half of malaria deaths every year. As these parasites develop resistance to current artemisinin-based therapies, people are vigorously developing new vaccines and preventive therapies.

　　Lead author Dhiia Moussaoui said: "The core of the malaria parasite liposome contains the essential myosin A motor (PfMyoA), which is the main target of current antimalarial drugs. PfMyoA is an active spore-like state of the parasite It is also an important molecule in the life cycle of the parasite, which can provide the required rapid motility and combine with the molecule’s conservative spherical motion domain and two "light" PfELC and MTIP. There is a lever arm to do it.

　　In their research, the Mousavi and Curie Institute team worked with the Trybus Institute at the University of Vermont to capture the first X-ray structure of a full-length PfMyoA motor in two states of Plasmodium falciparum. Their research shows that the unique activation of the PfMyoA lever arm is generated by the interaction of a specific lever arm/motion domain, allowing a larger power stroke to speed up the movement.

　　"" The lever arm usually contains an amino acid sequence called IQ that binds to the light chain of the molecule. In PfMyoA, the first IQ motif and the PfELC sequence bound to it are so degenerate that only recent studies have realized the existence of the essential light chain.

　　The team’s further analysis of the X-ray structure showed that PfELC is essential for Plasmodium falciparum to invade red blood cells, is a weak link in the assembly of a fully functional capsule, and may provide a new target for anti-malaria. display. Anne Houdusse, director of the Curie Institute, concluded: “The structure described here provides an accurate blueprint for the design of drugs targeting PfELC binding or PfMyoA full-length motor activity.” .. “This treatment The method reduces the function of the colloid and prevents the activity of the malaria parasite at the most infectious stage of its life cycle, thereby preventing the onset of the disease."