Shedding light on the hidden world of Leishmania 

Leishmania parasites, responsible for human leishmaniasis, are transmitted to humans through the bite of infected sandflies. These parasites can lead to chronic skin lesions and disfiguration, and in severe cases, may spread to internal organs, resulting in potentially life-threatening disease.

Our research focuses on how Leishmania controls gene expression, which occurs mainly at the level of protein synthesis. Through our studies, we found that the translation factors involved in protein synthesis present promising targets for new therapies. By identifying small molecules that disrupt protein-protein interactions specifically in Leishmania, we hope to contribute to the development of more effective and selective treatments for leishmaniasis.

Understanding protein synthesis in Apicomplexans

The Apicomplexa phylum includes some of the world’s most notorious parasites, responsible for diseases such as malaria, toxoplasmosis, and babesiosis. As drug resistance rises and current treatments remain limited—often accompanied by harsh side effects—the need for innovative and more effective therapies is more urgent than ever.

One groundbreaking strategy is to block the parasite’s ability to make proteins, mirroring how many antibiotics successfully target bacterial ribosomes. Excitingly, apicomplexan parasites house a fascinating organelle called the apicoplast. This unique structure is a relic of an ancient cyanobacterium, absorbed through an endosymbiotic event. The apicoplast’s ribosomes are distinctive—unlike any found in humans or animals—making them a highly promising target for next-generation antiparasitic drugs. Yet, much remains unknown about how apicomplexan ribosomes are built and regulated, which we aim to explore to open up bold new avenues for life-saving treatments.