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Apolipoprotein L-I Promotes Trypanosome Lysis by Forming Pores in Lysosomal Membranes
David Pérez-Morga,1*Benoit Vanhollebeke,1*Françoise Paturiaux-Hanocq,1Derek P. Nolan,2Laurence Lins,3Fabrice Homblé,4Luc Vanhamme,1Patricia Tebabi,1Annette Pays,1Philippe Poelvoorde,1Alain Jacquet,5Robert Brasseur,3Etienne Pays1
Apolipoprotein L-I is the trypanolytic factor of human serum.Here we show that this protein contains a membrane pore-formingdomain functionally similar to that of bacterial colicins, flankedby 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 andtriggered depolarization of this membrane, continuous influxof chloride, and subsequent osmotic swelling of the lysosomeuntil the trypanosome lysed.
1 Laboratory of Molecular Parasitology, IBMM, Université Libre de Bruxelles, 12, rue des Profs Jeener et Brachet, B6041 Gosselies, Belgium. 2 Department of Biochemistry, Trinity College, Dublin 2, Ireland. 3 Centre de Biophysique Moléculaire Numérique, Université de Gembloux, Belgium. 4 Structure et Fonction des Membranes Biologiques, Université Libre de Bruxelles, B1050 Brussels, Belgium. 5 Laboratory of Applied Genetics, IBMM, Université Libre de Bruxelles, B6041 Gosselies, Belgium.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: epays{at}ulb.ac.be
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