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Apolipoprotein L-I is the trypanosome lytic factor of human serum
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Journal Article
Apolipoprotein L-I is the trypanosome lytic factor of human serum
2003
Overview
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Apolipoproteins - metabolism
/ Apolipoproteins/blood/chemistry/metabolism
/ Biochemistry, biophysics & molecular biology
/ Biochimie, biophysique & biologie moléculaire
/ Glossina
/ Humanities and Social Sciences
/ Humans
/ letter
/ Lipoproteins, HDL - chemistry
/ Lipoproteins, HDL - metabolism
/ Lipoproteins, HDL/blood/chemistry/metabolism
/ Membrane Glycoproteins - chemistry
/ Membrane Glycoproteins - genetics
/ Membrane Glycoproteins - metabolism
/ Membrane Glycoproteins/chemistry/genetics/metabolism
/ Proteins
/ Science
/ Trypanosoma brucei rhodesiense
/ Trypanosoma brucei rhodesiense - metabolism
/ Trypanosoma brucei rhodesiense - pathogenicity
