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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Apolipoprotein L-I 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 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.[1]

References

  1. Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes. Pérez-Morga, D., Vanhollebeke, B., Paturiaux-Hanocq, F., Nolan, D.P., Lins, L., Homblé, F., Vanhamme, L., Tebabi, P., Pays, A., Poelvoorde, P., Jacquet, A., Brasseur, R., Pays, E. Science (2005) [Pubmed]
 
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