What is this publication about?

This publication presents the findings from research on Schistosoma parasites and their glycans, a specific class of molecules that trigger and modulate human host immune responses.

Researchers investigated how the molecular structure of protein-linked carbohydrate chains, known as N-glycans, can be altered in live Schistosoma mansoni worms to better understand the contribution of these glycans to survival of the parasite and the response of the human hosts. By using specific chemical inhibitors called kifunensine and swainsonine, scientists successfully blocked the natural processing of these N-glycans, resulting in remodelled glycoproteins in both the whole worm and its outer protective layer. Despite these significant and biochemically confirmed changes, the parasites maintained their normal movement and physical form during a two-week study period in culture.

Why is it important?

These glycans are believed to help the parasites evade the human immune system, which facilitates chronic infection and causes the tropical disease schistosomiasis. This study shows that glycan remodelling of Schistosoma worms for functional glycobiology studies is feasible, providing a new approach for exploring how specific glycans influence the complex relationship between the parasite and its host.    

How can this make a difference?

Schistosomiasis, a neglected tropical disease caused by Schistosoma worms, affects over 250 million people worldwide. In these infections, protective immunity generally develops only very slowly due to poorly understood mechanisms such as those modulated by glycans, and re-infections are therefore common. Studies such as this one help us better understand how immunity against worm infections can be developed, supporting the ongoing search for a vaccine against parasitic worms.