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The (neo-) lacto series glycosphingolipids (nsGSLs) comprise of glycan epitopes that are present as blood group antigens, act as primary receptors for human pathogens and are also increasingly associated with malignant diseases. Beta-1, 3- N -acetyl-glucosaminyl-transferase 5 (B3GNT5) is suggested as the key glycosyltransferase for the biosynthesis of nsGSLs. In this study, we investigated the impact of CRISPR- Cas9  -mediated gene disruption of  B3GNT5  (∆ B3GNT5 ) on the expression of glycosphingolipids and  N -glycoproteins by utilizing immunostaining and glycomics-based PGC-UHPLC-ESI-QTOF-MS/MS profiling. ∆ B3GNT5  cells lost nsGSL expression coinciding with reduction of α2-6 sialylation on  N -glycoproteins. In contrast, disruption of  B4GALNT1 , a glycosyltransferase for ganglio series GSLs did not affect α2-6 sialylation on  N -glycoproteins. We further profiled all known α2-6 sialyltransferase-encoding genes and showed that the loss of α2-6 sialylation is due to silencing of  ST6GAL1  expression in ∆ B3GNT5  cells. These results demonstrate that nsGSLs are part of a complex network affecting  N -glycosylation in ovarian cancer cells.

Altered (neo-) lacto series glycolipid biosynthesis impairs α2-6 sialylation on N-glycoproteins in ovarian cancer cells