Extended Data Fig. 2: Rip1 homologues provide defence against diverse phages.
From: A pore-forming antiphage defence is activated by oligomeric phage proteins
a, Sequence alignment of Rip1 homologues used in this study. Proteins were aligned using Clustal Omega and visualized with Jalview (v2.11.4.1). Residues are colored using the Clustal color scheme. Black triangles show conserved cysteine residues within the C4-type zinc-ribbon finger (highlighted by a solid black line). b, Percent pairwise amino acid sequence identity among Rip1 homologues. c, AlphaFold3 models of selected Rip1 homologues. d, Efficiency of plating (EOP) of T4-like phages and Bas3-like phages on MG1655 lawns with or without Rip1Eco. Data are shown as plaque-forming units (PFU) per mL. Bars show the mean ± SD (n = 3 biologically independent replicates). Each replicate is shown as an individual dot, and asterisks show statistically significant differences relative to plasmid control (*P value < 0.05 (unpaired two-tailed t-test)). Exact P values are provided in Source Data. e, Phage infection assays. Tenfold serial dilutions of indicated phages plated on MG1655 with or without Rip1Eco expression. f, EOP of Bas48-like phages on MG1655 with or without Rip1Vpa. Data are shown in PFU per mL. Bars show the mean ± SD (n = 3 biologically independent replicates). Each replicate is shown as an individual dot, and asterisks show statistically significant differences relative to plasmid control (*P value < 0.05 (unpaired two-tailed t-test)). Exact P values are provided in Source Data. g, Phage infection assays. Tenfold serial dilutions of indicated phages plated on MG1655 with and without Rip1Vpa. Bas47 on MG1655 EV is identical to that presented in panel e. Source Data are provided.
