Figure 2
ABMA inhibits cytotoxicity of several bacterial toxins. Cells were incubated with the indicated concentrations of ABMA and then challenged with increasing concentrations of the indicated toxins. (A) A549 cells were exposed to DT for 18 h. Culture media was removed and replaced with DMEM containing [14C]-leucine at 0.5 µCi/mL for 3 h before protein biosynthesis determination. (B) Immunoblots showing the levels of MEK2 in HUVEC cells left untreated (line 1) or treated with Anthrax LT (lines 2–3, LT = PA 3 µg/mL + LF 1 µg/mL) in the absence and presence of 30 µM of ABMA. Immmunoblot of anti-actin show equal protein loading. (C,D) Vero cells were intoxicated with TcdB for 4 h or TcsL for 18 h and morphological changes of intoxicated cells were imaged and analyzed. (E) HeLa cells were exposed to Stx2 for 16 h before protein biosynthesis determination as for DT. (F) ABMA or DMSO were added to rat cerebellar granule neurons (CGNs) 1 h prior to BoNT/A exposure (500 pM) in the presence of compounds for 24 h. Immunoblots showing the levels of SNAP-25 and its cleaved form in the absence and presence of ABMA. Immunoblots images from single experiment (B and E) were spliced to rearrange the order of samples. Full-length blots are presented in Supplementary Figure S8.
