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. Author manuscript; available in PMC: 2017 Aug 10.
Published in final edited form as: Cell Host Microbe. 2016 Jul 21;20(2):226–237. doi: 10.1016/j.chom.2016.06.010

Figure 5. Terminal fucosylation is required for T3SS2 cytotoxicity.

Figure 5

(A) Overview of the steps in the synthesis of fucosylated glycans, highlighting mutations conferring resistance to T3SS2 killing. (B) Flow cytometry profiles of HT-29 and mutant cells bound to fucose-specific FITC-conjugated lectins that recognize distinct fucosylation linkages. Charts below the graphs show geometric mean fluorescence intensity (GMFI). AAL, Aleuria aurantia; LTL, Lotus tetragonolobus; UEA-1, Ulex europaeus Iectin. (C) Kinetics of survival of HT-29 and mutant cells after infection with T3SS2+ or T3SS2− V. parahaemolyticus. (D). T3SS2 killing (top) and fucosylation (bottom) of wt, SLC35C1 mutant cells, and SLC35C1 mutant cells expressing an sgRNA resistant SLC35C1 cDNA. (E) Impact of the fucosylation inhibitor 2-FF on T3SS1 and T3SS2 killing of HT-29 cells. (F) Impact of 2-FF on survival of different cell lines infected with T3SS2+ V. parahaemolyticus. (G) Kinetics of cell survival following T3SS2+ V. parahaemolyticus infection of CHO parental and mutant cells. (H) Lectin binding profiles for CHO cells transduced with FUT genes that generate diverse terminal fucose linkages. Structures of the CHO cell N-glycan core and various terminal fucosylated blood group antigens are shown on the right. Data are mean with SEM (n=3), P values (* < =0.01, ** < 0.001) are based on one-way ANOVA with Dunnet post test correction.