Apolipoprotein L-1 Promotes Trypanosome Lysis By Forming Pores In Lysosomal Membranes

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 T...

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Main Authors Perez-Morga, David, Vanhollebeke, Benoit, Paturiaux-Hanocq, Françoise, Nolan, Derek P., Lins, Laurence, Homble, Fabrice, Vanhamme, Luc, Tebabi, Patricia, Pays, Annette, Poelvoorde, Philippe, Jacquet, Alain, Brasseur, Robert, Pays, Etienne
Format Web Resource
LanguageEnglish
Published American Association for the Advancement of Science 15.07.2005
Subjects
Biochemistry, biophysics & molecular biology
Biochimie, biophysique & biologie moléculaire
Life sciences
Sciences du vivant
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Summary: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.
Bibliography:scopus-id:2-s2.0-22344443961
ISSN:1095-9203
0036-8075
DOI:10.1126/science.1114566