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Apolipoprotein L-I Promotes Trypanosome Lysis by Forming Pores in Lysosomal Membranes

Science  15 Jul 2005:
Vol. 309, Issue 5733, pp. 469-472
DOI: 10.1126/science.1114566

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Abstract

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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