Major human schistosome species express different glycans with immunological and diagnostic implications.

Schistosomes are parasitic worms responsible for devastating chronic disease including intestinal and urogenital pathologies. In-depth studies of the Schistosoma mansoni glycome have revealed complex, immunogenic and life stage-specific glycans, that are crucial in host-parasite interactions. Despite causing the majority of schistosome infections and specific associated pathology, the glycosylation of S. haematobium remains largely unstudied. Here, we characterize the glycan repertoire of S. haematobium using mass spectrometry-based approaches. We report substantial differences to S. mansoni glycans, most notably in the core structure, fucosylation patterns and glucuronic acid modifications of glycosphingolipid (GSL) glycans. Furthermore, IgG from S. haematobium-infected individuals preferentially bind the acidic GSL glycans compared to IgG from S. mansoni-infected individuals. Our results demonstrate that S. haematobium and S. mansoni are differentially glycosylated and that S. haematobium glycans are involved in parasite-host immunobiology. The specific, immunogenic S. haematobium glycans constitute targets for use in epidemiological studies and potential species-specific diagnostics.