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. 2019 Feb 5;10(1):e02816-18. doi: 10.1128/mBio.02816-18

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FIG 4 — Levels of LC3 and p62 are elevated in infected cells and the proteins are efficiently degraded when autophagy is induced by starvation. (A) Immunoblot of lysates from THP-1 macrophages left uninfected (UI) or infected with wild-type C. burnetii (WT) or the ΔdotA mutant for 72 h in complete medium. Immunoblots were probed with antibodies against LC3, p62, EF-Ts, or actin. Plots depict means ± standard deviations of LC3 or p62 signal normalized to the actin loading control for three independent experiments. (B) Immunoblot of lysates from HeLa cells left uninfected (UI) or infected with wild-type C. burnetii (WT) for 72 h in complete medium (Comp) or subjected to continued incubation in HBSS for the indicated times. Immunoblots were probed with antibodies against LC3, p62, or actin. (C and D) Quantitation of LC3 (C) and p62 (D) signals in panel B. Plots depict means of signal data ± standard deviations of results from three independent experiments. Asterisks indicate statistical significance (*, P < 0.05; **, P < 0.01).