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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Thomson, Russell Finkelstein, Alan |
| Description | Author Affiliation: Thomson R ( Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461 rthomson@einstein.yu.edu.); Finkelstein A ( Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461.); |
| Abstract | Apolipoprotein L-1 (APOL1), the trypanolytic factor of human serum, can lyse several African trypanosome species including Trypanosoma brucei brucei, but not the human-infective pathogens T. brucei rhodesiense and T. brucei gambiense, which are resistant to lysis by human serum. Lysis follows the uptake of APOL1 into acidic endosomes and is apparently caused by colloid-osmotic swelling due to an increased ion permeability of the plasma membrane. Here we demonstrate that nanogram quantities of full-length recombinant APOL1 induce ideally cation-selective macroscopic conductances in planar lipid bilayers. The conductances were highly sensitive to pH: their induction required acidic pH (pH 5.3), but their magnitude could be increased 3,000-fold upon alkalinization of the milieu (pK(a) = 7.1). We show that this phenomenon can be attributed to the association of APOL1 with the bilayer at acidic pH, followed by the opening of APOL1-induced cation-selective channels upon pH neutralization. Furthermore, the conductance increase at neutral pH (but not membrane association at acidic pH) was prevented by the interaction of APOL1 with the serum resistance-associated protein, which is produced by T. brucei rhodesiense and prevents trypanosome lysis by APOL1. These data are consistent with a model of lysis that involves endocytic recycling of APOL1 and the formation of cation-selective channels, at neutral pH, in the parasite plasma membrane. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 9 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-03-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Apolipoproteins Pharmacology Cell Membrane Metabolism Lipid Bilayers Lipoproteins, HDL Trypanocidal Agents Trypanosoma Brucei Gambiense Chemistry Genetics Hydrogen-Ion Concentration Recombinant Proteins Research Support, N.I.H., Extramural Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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