Extended Data Fig. 3: MS/MS spectra of the cADPR isomer produced by ThsB following phage infection and the activity of the SLOG domain.
From: Antiviral activity of bacterial TIR domains via immune signalling molecules
a, MS/MS fragmentation spectra of standard cADPR (top) and the Thoeris-derived cADPR isomer (bottom). Hypothesized structures of MS/MS fragments of cADPR are presented. b, EOP of phages on bacteria expressing WT ThsB and ThsA(R371A) compared to WT Thoeris and other mutants. Results for the control, WT Thoeris and ThsB(E85Q) and ThsA(N112A) are those presented in Extended Data Fig. 1. Asterisk marks statistically significant reduction in EOP (One-way ANOVA, followed by pairwise multiple comparison analysis according to Tukey’s honest significant difference criterion p = 2*10−8). EOP of ThsA(R371A) is not statistically significant compared to the control strain (p = 0.7). c–f, Two additional replicates of the mass photometry measurement presented in Figs 3d, e. ThsA purified protein was incubated with lysates derived from infected cells expressing ThsB(E85Q) (c, e) or ThsB (d, f). Dashed lines represent masses of ThsA monomer, dimer and tetramer.
