American Association for the Advancement of Science
Perez-Morga D., Vanhollebeke B., Paturiaux-Hanocq F., Nolan D.P., Lins L., Homble F., Vanhamme L., Tebabi P., Pays A., Poelvoorde P., Jacquet A., Brasseur R., Pays E., Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes, Science, 309, 2005, 469, 472
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.
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