ORBi: Perez-Morga David - Apolipoprotein L-1 Promotes Trypanosome Lysis By Forming Pores In Lysosomal Membranes

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


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/63492

Title :	Apolipoprotein L-1 Promotes Trypanosome Lysis By Forming Pores In Lysosomal Membranes
Language :	English
Author, co-author :	Perez-Morga, David [> > > >]
	Vanhollebeke, Benoit [> > > >]
	Paturiaux-Hanocq, Françoise [> > > >]
	Nolan, Derek P. [> > > >]
	Lins, Laurence [Université de Liège > > Gembloux Agro-Bio Tech >]
	Homble, Fabrice [> > > >]
	Vanhamme, Luc [> > > >]
	Tebabi, Patricia [> > > >]
	Pays, Annette [> > > >]
	Poelvoorde, Philippe [> > > >]
	Jacquet, Alain [> > > >]
	Brasseur, Robert [Université de Liège > > Gembloux Agro-Bio Tech >]
	Pays, Etienne [> > > >]
Publication date :	2005
Journal title :	Science
Volume :	309
Issue/season :	5733
Pages :	469-72
Audience :	International
ISSN :	0036-8075
Abstract :	[en] 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.
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/63492
DOI :	10.1126/science.1114566

File(s) associated to this reference

Fulltext file(s):

	File	Commentary	Version	Size	Access
Restricted access	234-cv.pdf		Publisher postprint	391.66 kB	Request copy

All documents in ORBi are protected by a user license.