Fig. 5: SrfD interacts with host Sec61 and localizes to the ER via multiple domains. | Nature Communications

Fig. 5: SrfD interacts with host Sec61 and localizes to the ER via multiple domains.

From: Cell-selective proteomics reveal novel effectors secreted by an obligate intracellular bacterial pathogen

Fig. 5

a Proteins co-enriched following immunoprecipitation (IP) mass spectrometry of SrfD secreted by R. parkeri during infection of A549 cells. Protein abundance fold-changes and Benjamini–Hochberg adjusted p-values (padj) were computed for n = 3 independent infected (inf.) and uninfected (uninf.) samples (unpaired two-tailed t-test, df = 4). SrfD (blue), Sec61α/β (red), and thresholds for fold-change >4 and padj < 0.01 are indicated. b Western blots for SrfD and Sec61β following IP of Sec61β from A549 cells. Samples were prepared from R. parkeri-infected (inf.) and uninfected (uninf.) cells. c Western blots for FLAG and Sec61β following IP of Sec61β from HEK293T cells transiently transfected with 3xFLAG-tagged SrfD expression constructs. Putative domains and structural motifs are indicated. – empty vector, FL full-length SrfD. d Images of 3xFLAG-tagged SrfD constructs (cyan) from c expressed by transiently transfected HeLa cells (Sec61β, red). White indicates an overlap between FLAG and Sec61β signals. Scale bar, 10 μm. Results for (b–d) are representative of at least two independent experiments. Source data are provided as a Source Data file.

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