Fig. 5: Both the N- and C-terminal domains contribute to SSL10-induced necroptosis. | Communications Biology

Fig. 5: Both the N- and C-terminal domains contribute to SSL10-induced necroptosis.

From: Staphylococcal superantigen-like protein 10 induces necroptosis through TNFR1 activation of RIPK3-dependent signal pathways

Fig. 5

a The overall structure of SSL10. The OB-fold domain and β-grasp domain of SSL10 are colored magenta and green, respectively. b The electrostatic surface potentials of SSL10. Positively and negatively charged surface regions are colored blue and red, respectively. c Illustration of chimeric SSL variants used in this study. Blue and gray boxes represent sequences derived from SSL10 and SSL7, respectively. The numbers indicate the residue positions of the N- and C-terminus of the swapped domains. d LDH released from HEK293T cells treated with 2 μM SSL10, SSL7, SSL10 × 7, and SSL7 × 10. All data are presented as the means ± SD from three independent experiments. *p < 0.05; **p < 0.01 compared to the Ctrl cells (buffer-treated cells). #p < 0.05 compared to the SSL10 treated group, by one-way ANOVA. e MBP pull-down of SSL10, SSL7, SSL10 × 7 and SSL7 × 10 by MBP-TNFR1ECD.

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