The natural function of the malaria parasite’s chloroquine resistance transporter
Plasmodium falciparum chloroquine resistance transporter (PfCRT) mediates multidrug resistance, but its natural function remains unclear. Here, Shafik et al. show that PfCRT transports host-derived peptides of 4-11 residues but not other ions or metabolites, and that drug-resistance-conferring PfCRT...
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2020-08-01
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Online Access: | https://doi.org/10.1038/s41467-020-17781-6 |
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doaj-e62a9cfeb1b74e3793184dbfb72b16f72021-08-08T11:38:27ZengNature Publishing GroupNature Communications2041-17232020-08-0111111610.1038/s41467-020-17781-6The natural function of the malaria parasite’s chloroquine resistance transporterSarah H. Shafik0Simon A. Cobbold1Kawthar Barkat2Sashika N. Richards3Nicole S. Lancaster4Manuel Llinás5Simon J. Hogg6Robert L. Summers7Malcolm J. McConville8Rowena E. Martin9Research School of Biology, The Australian National UniversityBio21 Molecular Science and Biotechnology Institute, University of MelbourneResearch School of Biology, The Australian National UniversityResearch School of Biology, The Australian National UniversityResearch School of Biology, The Australian National UniversityDepartment of Biochemistry and Molecular Biology, Department of Chemistry, and Huck Center for Malaria Research, The Pennsylvania State UniversityResearch School of Biology, The Australian National UniversityResearch School of Biology, The Australian National UniversityBio21 Molecular Science and Biotechnology Institute, University of MelbourneResearch School of Biology, The Australian National UniversityPlasmodium falciparum chloroquine resistance transporter (PfCRT) mediates multidrug resistance, but its natural function remains unclear. Here, Shafik et al. show that PfCRT transports host-derived peptides of 4-11 residues but not other ions or metabolites, and that drug-resistance-conferring PfCRT mutants have reduced peptide transport.https://doi.org/10.1038/s41467-020-17781-6 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Sarah H. Shafik Simon A. Cobbold Kawthar Barkat Sashika N. Richards Nicole S. Lancaster Manuel Llinás Simon J. Hogg Robert L. Summers Malcolm J. McConville Rowena E. Martin |
spellingShingle |
Sarah H. Shafik Simon A. Cobbold Kawthar Barkat Sashika N. Richards Nicole S. Lancaster Manuel Llinás Simon J. Hogg Robert L. Summers Malcolm J. McConville Rowena E. Martin The natural function of the malaria parasite’s chloroquine resistance transporter Nature Communications |
author_facet |
Sarah H. Shafik Simon A. Cobbold Kawthar Barkat Sashika N. Richards Nicole S. Lancaster Manuel Llinás Simon J. Hogg Robert L. Summers Malcolm J. McConville Rowena E. Martin |
author_sort |
Sarah H. Shafik |
title |
The natural function of the malaria parasite’s chloroquine resistance transporter |
title_short |
The natural function of the malaria parasite’s chloroquine resistance transporter |
title_full |
The natural function of the malaria parasite’s chloroquine resistance transporter |
title_fullStr |
The natural function of the malaria parasite’s chloroquine resistance transporter |
title_full_unstemmed |
The natural function of the malaria parasite’s chloroquine resistance transporter |
title_sort |
natural function of the malaria parasite’s chloroquine resistance transporter |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2020-08-01 |
description |
Plasmodium falciparum chloroquine resistance transporter (PfCRT) mediates multidrug resistance, but its natural function remains unclear. Here, Shafik et al. show that PfCRT transports host-derived peptides of 4-11 residues but not other ions or metabolites, and that drug-resistance-conferring PfCRT mutants have reduced peptide transport. |
url |
https://doi.org/10.1038/s41467-020-17781-6 |
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