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. 2014 Jun 13;462:1–13. doi: 10.1016/j.virol.2014.05.022

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Copyright © 2014 Elsevier Inc. All rights reserved.

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Fig. 6 — Manipulation of phospholipids metabolism regulates protein A-induced (+)RNA1E recruitment in cells. (A,B) Measurement of PA and PC content in Pr-E cells treated with 100 nM FIPI (A) and 50 μM miltefosine (B) or with matching concentration of DMSO (vehicle). (C) Viability of cells treated with FIPI, miltefosine or DMSO. (D) FIPI or miltefosine treatment show less effect on the activity of mitochondrial membrane-binding protein to associate with membranes. Nycodenz flotation assay were used to examine membrane association of protein A and porin in cells treated with FIPI, miltefosine or DMSO. LD fractions represent the membrane-rich layers in the gradient, whereas the HD (non-membrane) fractions contain cytosolic soluble proteins. (E) (+)RNA1E accumulation in cells treated with FIPI, miltefosine or DMSO expressing protein A_GAA-HA. Cells were divided into two equal fractions. One of fractions was analyzed by Northern blotting with EGFP and 18 s rRNA probes, respectively. The other fraction was analyzed by Western blotting with anti-HA and anti-GAPDH antibodies, respectively. GAPDH, glyceraldehyde-3-phosphate dehydrogenase. (F) Quantification data show the accumulation of (+)RNA1E and protein A in Pr-E cells expressing protein A_GAA-HA treated with FIPI, miltefosine or DMSO, respectively. The accumulation of RNA and protein is normalized to 18S rRNA and GAPDH, respectively. Error bars represent S.D. values from at least three independent experiments.