Apolipoprotein L-I is the trypanosome lytic factor of human serum

Luc Vanhamme, Françoise Paturiaux-Hanocq, Philippe Poelvoorde, Derek P. Nolan, Laurence Lins, Jan Van Den Abbeele, Annette Pays, Patricia Tebabi, Huang Van Xong, Alain Jacquet, Nicole Moguilevsky, Marc Dieu, John P. Kane, Patrick De Baetselier, Robert Brasseur and Etienne Pays ()
Additional contact information
Luc Vanhamme: University of Brussels
Françoise Paturiaux-Hanocq: University of Brussels
Philippe Poelvoorde: University of Brussels
Derek P. Nolan: University of Brussels
Laurence Lins: University of Gembloux
Jan Van Den Abbeele: Institute for Tropical Medicine
Annette Pays: University of Brussels
Patricia Tebabi: University of Brussels
Huang Van Xong: Free University of Brussels
Alain Jacquet: University of Brussels
Nicole Moguilevsky: University of Brussels
Marc Dieu: University of Namur
John P. Kane: University of California
Patrick De Baetselier: Free University of Brussels
Robert Brasseur: University of Gembloux
Etienne Pays: University of Brussels

Nature, 2003, vol. 422, issue 6927, 83-87

Abstract: Abstract Human sleeping sickness in east Africa is caused by the parasite Trypanosoma brucei rhodesiense. The basis of this pathology is the resistance of these parasites to lysis by normal human serum (NHS)1,2. Resistance to NHS is conferred by a gene that encodes a truncated form of the variant surface glycoprotein termed serum resistance associated protein (SRA)3,4. We show that SRA is a lysosomal protein, and that the amino-terminal α-helix of SRA is responsible for resistance to NHS. This domain interacts strongly with a carboxy-terminal α-helix of the human-specific serum protein apolipoprotein L-I (apoL-I). Depleting NHS of apoL-I, by incubation with SRA or anti-apoL-I, led to the complete loss of trypanolytic activity. Addition of native or recombinant apoL-I either to apoL-I-depleted NHS or to fetal calf serum induced lysis of NHS-sensitive, but not NHS-resistant, trypanosomes. Confocal microscopy demonstrated that apoL-I is taken up through the endocytic pathway into the lysosome. We propose that apoL-I is the trypanosome lytic factor of NHS, and that SRA confers resistance to lysis by interaction with apoL-I in the lysosome.

Date: 2003
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DOI: 10.1038/nature01461

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