Schistosomes are parasitic worms responsible for devastating chronic diseases worldwide. Schistosoma mansoni and S. haematobium are the major species infecting humans, causing intestinal and urogenital pathologies, respectively. The S. mansoni glycome has been studied in detail, revealing complex, immunogenic and life stage-specific glycans crucial in host-parasite interactions. Very little is known, however, regarding the glycosylation and glycan antigenicity for other schistosome species, including S. haematobium which is estimated to be responsible for half of the approximately 250 million schistosome infections. Thus, we investigated the glycans expressed on cercariae, worms and eggs of S. haematobium. First, protein and lipid-linked glycans were released using enzymatic and chemical techniques and characterized using mass-spectrometry (MS) based approaches. Glycan structures were determined using sequencing techniques including exoglycosidase digestions in combination with MALDI-TOF-MS, and porous graphitized carbon-liquid chromatography-MS for in-depth resolution of complex isomeric structures. Our analysis revealed substantial differences between S. haematobium and S. mansoni glycosylation. Notably, S. haematobium glycosphingolipid (GSL) glycans are built on a trihexosyl core unlike the disaccharide core described in S. mansoni, are enriched in terminal acidic residues, but present a lower degree of fucosylation. The protein-linked glycans, on their hand, present core-modifications and terminal motifs identical to S. mansoni, although expressed with major quantitative differences. Next, a selection of glycans representative of S. haematobium and S. mansoni glycomes including a broad coverage of the differential structures was purified and printed on a glycan microarray. Upon array screening, we observed a strong binding to acidic GSL glycans of IgG in sera from S. haematobium-infected individuals compared to S. mansoni-infected individuals and uninfected controls. These results indicate that the species-specific glycans characterized in S. haematobium are immunogenic and may play a role in S. haematobium specific immunobiology and pathology. Additionally, they constitute a potential diagnostic target specific for S. haematobium infections.