Microbiology: Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes

Science

Volumn 309, Issue 5733, 2005, Pages 469-472

  Pérez Morga, David ^a   Vanhollebeke, Benoit ^a   Paturiaux Hanocq, Françoise ^a   Nolan, Derek P ^b   Lins, Laurence ^c   Homblé, Fabrice ^a   Vanhamme, Luc ^a   Tebabi, Patricia ^a   Pays, Annette ^a   Poelvoorde, Philippe ^a   Jacquet, Alain ^a   Brasseur, Robert ^c   Pays, Etienne ^a  

^a UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

^b TRINITY COLLEGE DUBLIN   (Ireland)

^c UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOLOGICAL MEMBRANES; LIPIDS; POLARIZATION;

APOLIPOPROTEIN L-I; HUMAN SERUM; TRYPANOLYTIC FACTORS;

PROTEINS;

ANION CHANNEL; APOLIPOPROTEIN; APOLIPOPROTEIN L1; COLICIN; UNCLASSIFIED DRUG; 4,4' DIISOTHIOCYANATOSTILBENE 2,2' DISULFONIC ACID; ANION; APOL1 PROTEIN, HUMAN; CHLORIDE; HIGH DENSITY LIPOPROTEIN; ION CHANNEL; RECOMBINANT PROTEIN;

PROTEIN;

ARTICLE; BILAYER MEMBRANE; CHLORIDE TRANSPORT; CYTOLYSIS; DNA FLANKING REGION; GENE TARGETING; LYSOSOME MEMBRANE; MEMBRANE DEPOLARIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; TRYPANOSOMA; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECT; ESCHERICHIA COLI; GENETICS; GROWTH, DEVELOPMENT AND AGING; HUMAN; IMMOBILIZED CELL; INTRACELLULAR MEMBRANE; LIPID BILAYER; LYSOSOME; METABOLISM; MOLECULAR GENETICS; MUTATION; PERMEABILITY; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; TRYPANOSOMA BRUCEI; ULTRASTRUCTURE;

TRYPANOSOMA; TRYPANOSOMA BRUCEI;

4,4'-DIISOTHIOCYANOSTILBENE-2,2'-DISULFONIC ACID; AMINO ACID SEQUENCE; ANIMALS; ANIONS; APOLIPOPROTEINS; CELLS, IMMOBILIZED; CHLORIDES; COLICINS; ESCHERICHIA COLI; HUMANS; INTRACELLULAR MEMBRANES; ION CHANNELS; LIPID BILAYERS; LIPOPROTEINS, HDL; LYSOSOMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PERMEABILITY; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; TRYPANOSOMA BRUCEI BRUCEI;

EID: 22344443961     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1114566     Document Type: Article

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24. We thank D. Duché (Marseille) for the gift of plasmids; K. Zouaoui Boudjeltia and M. Vanhaeverbeek (Vésale Charleroi) for help in collecting NHS; C. Vansanten, F. Delfosse, E. Dupont, C. Felu, and M. Magi for assistance; and C. Vandenbussche and C. Miller for advice. This work was supported by the Belgian National Fund for Scientific Research (FNRS, FRSM, and Crédit aux Chercheurs), the United Nations Development Program/World Bank/World Health Organization Special Programme for Research and Training in Tropical Diseases, and the Communauté Française de Belgique-Action de Recherches Concertées and the Interuniversity Attraction Poles Programme-Belgian Science Policy. F.H. and R.B. are Research Directors, L.V. and L.L. are Research Associates, and B.V. is a Research Fellow, all at the FNRS; D.P.N. is a senior fellow of the Wellcome Trust.