Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes.
Science
; 309(5733): 469-72, 2005 Jul 15.
Article
in En
| MEDLINE
| ID: mdl-16020735
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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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Apolipoproteins
/
Trypanosoma brucei brucei
/
Intracellular Membranes
/
Lipoproteins, HDL
/
Lysosomes
Type of study:
Prognostic_studies
Language:
En
Journal:
Science
Year:
2005
Type:
Article
Affiliation country:
Belgium