Proximity-dependent proteomics of the Chlamydia trachomatis inclusion membrane reveals functional interactions with endoplasmic reticulum exit sites
Fig 2
Global analysis of the inclusion membrane interaction proteome throughout the C. trachomatis developmental cycle.
(A) Heatmap of inclusion membrane interacting proteome identified by APEX2 at 8, 16, and 24 hpi. Data from 6 replicate experiments per time point were averaged and compared against 6 replicate controls at similar times. Colors represent p-values, proteins not detected have no color. Enlarged section of heatmap shows proteins significantly enriched at all time points. Significance determined by t-test or g-test, p < 0.05. (B) C. trachomatis ORFs identified on the inclusion membrane, with p values displayed for their presence in 6 replicate samples for each time point. Locus tags highlighted in green represent annotated Inc proteins. Values highlighted in blue represent p values < 0.05. (C) KEGG pathway overrepresentation analysis of inclusion membrane proteome. Overrepresentation determined by hypergeometric algorithm with Benjamini Hochberg method for multiple test correction. Values highlighted in blue represent p values < 0.05. (D) Subcellular location enrichments of APEX2 identified proteins. Color intensity reflects the number of proteins for each location annotation pulled from the Human Protein Atlas database. Numbers in parentheses indicate the total number of reference proteins contained under that annotation in the Human Protein Atlas database. (E) Spatial distribution of inclusion interacting proteins from 8–24 hpi using Human Protein Atlas annotations and manual entry of Inc proteins. Color intensity indicates the number of proteins assigned to location annotations. A, actin filaments; Cy, cytosol; E, endosomes; ER, endoplasmic reticulum; Ex, extracellular/secreted; G, Golgi apparatus; IM, inclusion membrane; L, lysosomes; LD, lipid droplets; M, mitochondria; MT, microtubules; MTOC, microtubule organizing center; N, nucleus; P, peroxisomes; PM, plasma membrane; V, vesicles.