Extended Data Figure 5: The LRR domain in IpaH9.8 mediates hGBP1 binding that is independent of the nucleotide-bound states of hGBP1.
From: Ubiquitination and degradation of GBPs by a Shigella effector to suppress host defence
a, c, d, Gel filtration chromatography analyses of in vitro complex formation between the LRR domain of IpaH9.8 and hGBP1 (a) and between IpaH9.8 and wild-type (c), R48A or D184N mutant (d) hGBP1. Purified hGBP1 was pre-incubated with GMP, GDP, GppNHp, or GDP–AlFx. b, Flag–IpaH9.8 and haemagglutinin (HA)-tagged hGBP1 or hGBP5 were co-expressed in 293T cells. Lysates were immunoprecipitated with Flag antibody (Flag IP), and immunoblotted as shown. e, In vitro ubiquitination of the R48A, D184N and C589S mutants of hGBP1 by IpaH9.8. All data shown are representative of three independent experiments.
