Journal
SCIENCE
Volume 309, Issue 5733, Pages 469-472Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1114566
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- Wellcome Trust Funding Source: Medline
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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 bacteria[ 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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