R. Cahan et al., A 28,000 MOL-WT TOXIN FROM BACILLUS-THURINGIENSIS ISRAELENSIS INDUCESCATION-TRANSPORT IN RAT MUSCLE CULTURES, Toxicon, 33(7), 1995, pp. 943-951
The mechanism by which the Bacillus thuringiensis israelensis (Bti) 28
,000 mel. wt toxin exerts its effect on mature muscle cultures was exa
mined. The toxin inhibited Na+/K+-ATPase activity as revealed by Rb-86
influx. A 50% inhibition of Na+/K+-ATPase activity was obtained with
0.2 mu g/ml of the toxin. The inhibition was time and dose dependent,
and it was reversible with low doses of the toxin (up to 0.2 mu g/ml.
A considerable release of Rb-86 was obtained by doses greater than 0.2
mu g/ml. The Rb-86 release was also time and dose dependent. This eff
ect is probably non-specific, since Ca-45 influx is also accelerated b
y toxin-treated cultures. Pre-incubation of the toxin with phosphotidy
lserine (PS) antagonized the toxin. It is concluded that the toxin is
a hydrophobic protein which interacts with the membrane. In low doses
this interaction reduces the activity of the sodium pump and in high d
oses it causes non-specific permeability of the sarcolemma.