Apolipoprotein LI promotes trypanosome lysis by forming pores in lysosomal membranes
D Pérez-Morga, B Vanhollebeke, F Paturiaux-Hanocq… - Science, 2005 - science.org
Science, 2005•science.org
Apolipoprotein LI is the trypanolytic factor of human serum. Here we show that this protein
contains a membrane pore-forming domain functionally similar to that of bacterial colicins,
flanked by a membrane-addressing domain. In lipid bilayer membranes, apolipoprotein LI
formed anion channels. In Trypanosoma brucei, apolipoprotein LI was targeted to the
lysosomal membrane and triggered depolarization of this membrane, continuous influx of
chloride, and subsequent osmotic swelling of the lysosome until the trypanosome lysed.
contains a membrane pore-forming domain functionally similar to that of bacterial colicins,
flanked by a membrane-addressing domain. In lipid bilayer membranes, apolipoprotein LI
formed anion channels. In Trypanosoma brucei, apolipoprotein LI was targeted to the
lysosomal membrane and triggered depolarization of this membrane, continuous influx of
chloride, and subsequent osmotic swelling of the lysosome until the trypanosome lysed.
Apolipoprotein L-I is the trypanolytic factor of human serum. Here we show that this protein contains a membrane pore-forming domain functionally similar to that of bacterial colicins, flanked by a membrane-addressing domain. In lipid bilayer membranes, apolipoprotein L-I formed anion channels. In Trypanosoma brucei, apolipoprotein L-I was targeted to the lysosomal membrane and triggered depolarization of this membrane, continuous influx of chloride, and subsequent osmotic swelling of the lysosome until the trypanosome lysed.
AAAS