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. 2018 May 22;86(6):e00123-18. doi: 10.1128/IAI.00123-18

FIG 1.

FIG 1

Actin polymerization of R. parkeri in Vero and ISE6 cells and expression of Sca2 and RickA in ISE6 cells. (A and B) Wild-type R. parkeri (green) polymerizing actin (magenta) in Vero cells at 30 mpi and 48 hpi. (C and D) Wild-type R. parkeri (green) polymerizing actin (magenta) in ISE6 cells 30 mpi and 48 hpi. White scale bar, 2 μm. Arrows indicate Rickettsia polymerizing actin. (E) Percentage of wild-type R. parkeri present in Vero and ISE6 cells with an actin tail at 30 mpi and 2, 24, and 48 hpi. Bacteria with and without actin tails were recorded at each time point postinfection in order to determine the profile of R. parkeri actin polymerization. Error bars represent the standard errors of the means. Data are representative of two replicates per experiment and two independent experiments. Ten images taken across all experimental replicates were used in analyses. (F and G) Western blot (F) and corresponding graph (G) of RickA expression normalized against ISE6 expression of β-actin at 30 mpi and 8 and 48 hpi for wild-type R. parkeri. (H and I) Western blot (H) and corresponding graph (I) of Sca2 expression normalized against ISE6 expression of β-actin at 30 mpi and 8 and 48 hpi for wild-type R. parkeri. Statistical analysis consisted of a one-way ANOVA followed by Tukey's post hoc analysis (G and I) or an unpaired t test (E), with a P value of <0.05 considered significant (denoted by an asterisk). Data are representative of two replicates per experiment and two independent experiments.