Fig. 6

Change of expression of genes encoding glycosyltransferases catalyzing the synthesis of glycan cores [1,2,3,4] in PIEs infected with RVC, G9P[13] and G5P[7] versus control (non-infected PIEs). O-glycan development is a sequential process which requires the activity of several enzymes belonging to glycosyltransferase family. The initial step of mucin-type O-glycosylation in mammals (addition of GalNAc to PTS domain—Tn antigen) is provided by the activity of N-acetylgalactosaminyltransferases (ppGalNAc-Ts)—enzymes which are encoded by one of 20 genes. This antigen is further extended to glycan cores by addition of different carbohydrate residues including N-acetylgalactosamine (GalNAc), galactose (Gal), N-acetylglucosamine (GlcNAc), fucose (Fuc) and SA provided by activity of different glycosyltransferases. These extended glycan core structures can be included in the structure of secreted or transmembrane mucins MUC1, MUC2, MUC5AC, MUC5B, MUC6-8, MUC 11-13 and MUC 16 (79). Bars indicate fold change difference between infected PIEs vs uninfected control. Black circles represent the significance (p-value < 0.05, i.e. 1.3 in − log10 format)