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News
Scientists have discovered that lysine methylation — a chemical modification typically associated with gene regulation — directly controls how parasites like Toxoplasma gondii and Plasmodium falciparum move and invade host cells. Two enzymes act in sequence to activate the parasite's motility machinery. Because these enzymes are unique to parasites, they could be prime targets for new antiparasitic drugs.
Researchers at LMU Munich have uncovered a surprising molecular mechanism that flips the "go" switch for some of the world's most dangerous parasites. In Toxoplasma gondii (the cause of toxoplasmosis) and Plasmodium falciparum (the malaria parasite), two enzymes called lysine methyltransferases work in sequence to activate the parasite's movement and invasion machinery — a process that was previously poorly understood.
The first enzyme, PCKMT, positions a key protein called Formin-1 at the parasite's tip, triggering local assembly of actin filaments and the protrusion of a specialized invasion structure. A second enzyme, AKMT, then links that actin network to the force-generating machinery. When PCKMT was removed in experiments, parasites lost the ability to move, exit host cells, or invade new ones.
Key Takeaways:
Why it matters: Malaria and toxoplasmosis collectively affect hundreds of millions of people globally. Identifying parasite-specific molecular switches opens a new avenue for drug development that could disrupt infection without harming the host.
