PfCRT and the trans‐vacuolar proton electrochemical gradient: regulating the access of chloroquine to ferriprotoporphyrin IX

Summary It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus has not yet been reached on the mechanism by which resistance is achieved. CQ‐resistant (CQR) parasite lines accumulate less CQ than do CQ‐sens...

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Published inMolecular microbiology Vol. 62; no. 1; pp. 238 - 251
Main Authors Bray, Patrick G., Mungthin, Mathirut, Hastings, Ian M., Biagini, Giancarlo A., Saidu, Dauda K., Lakshmanan, Viswanathan, Johnson, David J., Hughes, Ruth H., Stocks, Paul A., O'Neill, Paul M., Fidock, David A., Warhurst, David C., Ward, Stephen A.
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 01.10.2006
Blackwell Science
Subjects
Amino acids
Animals
Biological and medical sciences
Chloroquine - metabolism
Chloroquine - pharmacology
Drug Resistance - genetics
Fundamental and applied biological sciences. Psychology
Genes
Genotype & phenotype
Glucose - metabolism
Hemin - metabolism
Membrane Transport Proteins - genetics
Membrane Transport Proteins - physiology
Microbiology
Mutation
Mutation - genetics
Parasites
Parasitic Sensitivity Tests
Plasmodium falciparum
Plasmodium falciparum - drug effects
Plasmodium falciparum - genetics
Plasmodium falciparum - metabolism
Protons
Protozoan Proteins - genetics
Protozoan Proteins - physiology
Vacuoles - metabolism
Antimalarial
Parasiticide
Antirheumatic agent
Microbiology
Chloroquine
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Abstract Summary It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus has not yet been reached on the mechanism by which resistance is achieved. CQ‐resistant (CQR) parasite lines accumulate less CQ than do CQ‐sensitive (CQS) parasites. The CQR phenotype is complex with a component of reduced energy‐dependent CQ uptake and an additional component that resembles energy‐dependent CQ efflux. Here we show that the required energy input is in the form of the proton electrochemical gradient across the digestive vacuole (DV) membrane. Collapsing the DV proton gradient (or starving the parasites of glucose) results in similar levels of CQ accumulation in CQS and CQR lines. Under these conditions the accumulation of CQ is stimulated in CQR parasite lines but is reduced in CQS lines. Energy deprivation has no effect on the rate of CQ efflux from CQR lines implying that mutant PfCRT does not function as an efflux pump or active carrier. Using pfcrt‐modified parasite lines we show that the entire CQ susceptibility phenotype is switched by the single K76T amino acid change in PfCRT. The efflux of CQ in CQR lines is not directly coupled to the energy supply, consistent with a model in which mutant PfCRT functions as a gated channel or pore, allowing charged CQ species to leak out of the DV.
AbstractList It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus has not yet been reached on the mechanism by which resistance is achieved. CQ-resistant (CQR) parasite lines accumulate less CQ than do CQ-sensitive (CQS) parasites. The CQR phenotype is complex with a component of reduced energy-dependent CQ uptake and an additional component that resembles energy-dependent CQ efflux. Here we show that the required energy input is in the form of the proton electrochemical gradient across the digestive vacuole (DV) membrane. Collapsing the DV proton gradient (or starving the parasites of glucose) results in similar levels of CQ accumulation in CQS and CQR lines. Under these conditions the accumulation of CQ is stimulated in CQR parasite lines but is reduced in CQS lines. Energy deprivation has no effect on the rate of CQ efflux from CQR lines implying that mutant PfCRT does not function as an efflux pump or active carrier. Using pfcrt-modified parasite lines we show that the entire CQ susceptibility phenotype is switched by the single K76T amino acid change in PfCRT. The efflux of CQ in CQR lines is not directly coupled to the energy supply, consistent with a model in which mutant PfCRT functions as a gated channel or pore, allowing charged CQ species to leak out of the DV. [PUBLICATION ABSTRACT]
It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus has not yet been reached on the mechanism by which resistance is achieved. CQ-resistant (CQR) parasite lines accumulate less CQ than do CQ-sensitive (CQS) parasites. The CQR phenotype is complex with a component of reduced energy-dependent CQ uptake and an additional component that resembles energy-dependent CQ efflux. Here we show that the required energy input is in the form of the proton electrochemical gradient across the digestive vacuole (DV) membrane. Collapsing the DV proton gradient (or starving the parasites of glucose) results in similar levels of CQ accumulation in CQS and CQR lines. Under these conditions the accumulation of CQ is stimulated in CQR parasite lines but is reduced in CQS lines. Energy deprivation has no effect on the rate of CQ efflux from CQR lines implying that mutant PfCRT does not function as an efflux pump or active carrier. Using pfcrt-modified parasite lines we show that the entire CQ susceptibility phenotype is switched by the single K76T amino acid change in PfCRT. The efflux of CQ in CQR lines is not directly coupled to the energy supply, consistent with a model in which mutant PfCRT functions as a gated channel or pore, allowing charged CQ species to leak out of the DV.
It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus has not yet been reached on the mechanism by which resistance is achieved. CQ-resistant (CQR) parasite lines accumulate less CQ than do CQ-sensitive (CQS) parasites. The CQR phenotype is complex with a component of reduced energy-dependent CQ uptake and an additional component that resembles energy-dependent CQ efflux. Here we show that the required energy input is in the form of the proton electrochemical gradient across the digestive vacuole (DV) membrane. Collapsing the DV proton gradient (or starving the parasites of glucose) results in similar levels of CQ accumulation in CQS and CQR lines. Under these conditions the accumulation of CQ is stimulated in CQR parasite lines but is reduced in CQS lines. Energy deprivation has no effect on the rate of CQ efflux from CQR lines implying that mutant PfCRT does not function as an efflux pump or active carrier. Using pfcrt-modified parasite lines we show that the entire CQ susceptibility phenotype is switched by the single K76T amino acid change in PfCRT. The efflux of CQ in CQR lines is not directly coupled to the energy supply, consistent with a model in which mutant PfCRT functions as a gated channel or pore, allowing charged CQ species to leak out of the DV.It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus has not yet been reached on the mechanism by which resistance is achieved. CQ-resistant (CQR) parasite lines accumulate less CQ than do CQ-sensitive (CQS) parasites. The CQR phenotype is complex with a component of reduced energy-dependent CQ uptake and an additional component that resembles energy-dependent CQ efflux. Here we show that the required energy input is in the form of the proton electrochemical gradient across the digestive vacuole (DV) membrane. Collapsing the DV proton gradient (or starving the parasites of glucose) results in similar levels of CQ accumulation in CQS and CQR lines. Under these conditions the accumulation of CQ is stimulated in CQR parasite lines but is reduced in CQS lines. Energy deprivation has no effect on the rate of CQ efflux from CQR lines implying that mutant PfCRT does not function as an efflux pump or active carrier. Using pfcrt-modified parasite lines we show that the entire CQ susceptibility phenotype is switched by the single K76T amino acid change in PfCRT. The efflux of CQ in CQR lines is not directly coupled to the energy supply, consistent with a model in which mutant PfCRT functions as a gated channel or pore, allowing charged CQ species to leak out of the DV.
Summary It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus has not yet been reached on the mechanism by which resistance is achieved. CQ‐resistant (CQR) parasite lines accumulate less CQ than do CQ‐sensitive (CQS) parasites. The CQR phenotype is complex with a component of reduced energy‐dependent CQ uptake and an additional component that resembles energy‐dependent CQ efflux. Here we show that the required energy input is in the form of the proton electrochemical gradient across the digestive vacuole (DV) membrane. Collapsing the DV proton gradient (or starving the parasites of glucose) results in similar levels of CQ accumulation in CQS and CQR lines. Under these conditions the accumulation of CQ is stimulated in CQR parasite lines but is reduced in CQS lines. Energy deprivation has no effect on the rate of CQ efflux from CQR lines implying that mutant PfCRT does not function as an efflux pump or active carrier. Using pfcrt ‐modified parasite lines we show that the entire CQ susceptibility phenotype is switched by the single K76T amino acid change in PfCRT. The efflux of CQ in CQR lines is not directly coupled to the energy supply, consistent with a model in which mutant PfCRT functions as a gated channel or pore, allowing charged CQ species to leak out of the DV.
It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus has not yet been reached on the mechanism by which resistance is achieved. CQ-resistant (CQR) parasite lines accumulate less CQ than do CQ-sensitive (CQS) parasites. The CQR phenotype is complex with a component of reduced energy-dependent CQ uptake and an additional component that resembles energy-dependent CQ efflux. Here we show that the required energy input is in the form of the proton electrochemical gradient across the digestive vacuole (DV) membrane. Collapsing the DV proton gradient (or starving the parasites of glucose) results in similar levels of CQ accumulation in CQS and CQR lines. Under these conditions the accumulation of CQ is stimulated in CQR parasite lines but is reduced in CQS lines. Energy deprivation has no effect on the rate of CQ efflux from CQR lines implying that mutant PfCRT does not function as an efflux pump or active carrier. Using pfcrt -modified parasite lines we show that the entire CQ susceptibility phenotype is switched by the single K76T amino acid change in PfCRT. The efflux of CQ in CQR lines is not directly coupled to the energy supply, consistent with a model in which mutant PfCRT functions as a gated channel or pore, allowing charged CQ species to leak out of the DV.
Summary It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus has not yet been reached on the mechanism by which resistance is achieved. CQ‐resistant (CQR) parasite lines accumulate less CQ than do CQ‐sensitive (CQS) parasites. The CQR phenotype is complex with a component of reduced energy‐dependent CQ uptake and an additional component that resembles energy‐dependent CQ efflux. Here we show that the required energy input is in the form of the proton electrochemical gradient across the digestive vacuole (DV) membrane. Collapsing the DV proton gradient (or starving the parasites of glucose) results in similar levels of CQ accumulation in CQS and CQR lines. Under these conditions the accumulation of CQ is stimulated in CQR parasite lines but is reduced in CQS lines. Energy deprivation has no effect on the rate of CQ efflux from CQR lines implying that mutant PfCRT does not function as an efflux pump or active carrier. Using pfcrt‐modified parasite lines we show that the entire CQ susceptibility phenotype is switched by the single K76T amino acid change in PfCRT. The efflux of CQ in CQR lines is not directly coupled to the energy supply, consistent with a model in which mutant PfCRT functions as a gated channel or pore, allowing charged CQ species to leak out of the DV.
Author Lakshmanan, Viswanathan
Biagini, Giancarlo A.
Bray, Patrick G.
Hastings, Ian M.
O'Neill, Paul M.
Stocks, Paul A.
Mungthin, Mathirut
Fidock, David A.
Saidu, Dauda K.
Johnson, David J.
Hughes, Ruth H.
Warhurst, David C.
Ward, Stephen A.
AuthorAffiliation 1 Department of Molecular and Biochemical Parasitology, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool L3 5QA, UK
3 Cancer Center, NYU School of Medicine, 522 First Avenue, Smilow 1307, New York, NY 10016, USA
2 Phramongkutklao College of Medicine, Bangkok 10400, Thailand
6 ITD, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK
5 Department of Chemistry, University of Liverpool, Liverpool L69 7ZD, UK
4 Department of Microbiology and Immunology, Albert Einstein College of Medicine, Forchheimer 403, 1300 Morris Park Ave, the Bronx, NY 10461, USA
AuthorAffiliation_xml – name: 3 Cancer Center, NYU School of Medicine, 522 First Avenue, Smilow 1307, New York, NY 10016, USA
– name: 1 Department of Molecular and Biochemical Parasitology, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool L3 5QA, UK
– name: 4 Department of Microbiology and Immunology, Albert Einstein College of Medicine, Forchheimer 403, 1300 Morris Park Ave, the Bronx, NY 10461, USA
– name: 5 Department of Chemistry, University of Liverpool, Liverpool L69 7ZD, UK
– name: 6 ITD, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK
– name: 2 Phramongkutklao College of Medicine, Bangkok 10400, Thailand
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  givenname: Patrick G.
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  givenname: Viswanathan
  surname: Lakshmanan
  fullname: Lakshmanan, Viswanathan
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  givenname: David J.
  surname: Johnson
  fullname: Johnson, David J.
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  givenname: David C.
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  surname: Ward
  fullname: Ward, Stephen A.
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Issue 1
Keywords Antimalarial
Parasiticide
Antirheumatic agent
Microbiology
Chloroquine
Language English
License CC BY 4.0
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Blackwell Science
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SSID ssj0013063
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Snippet Summary It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus...
It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus has not...
Summary It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus...
It is accepted that resistance of Plasmodium falciparum to chloroquine (CQ) is caused primarily by mutations in the pfcrt gene. However, a consensus has not...
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SubjectTerms Amino acids
Animals
Biological and medical sciences
Chloroquine - metabolism
Chloroquine - pharmacology
Drug Resistance - genetics
Fundamental and applied biological sciences. Psychology
Genes
Genotype & phenotype
Glucose - metabolism
Hemin - metabolism
Membrane Transport Proteins - genetics
Membrane Transport Proteins - physiology
Microbiology
Mutation
Mutation - genetics
Parasites
Parasitic Sensitivity Tests
Plasmodium falciparum
Plasmodium falciparum - drug effects
Plasmodium falciparum - genetics
Plasmodium falciparum - metabolism
Protons
Protozoan Proteins - genetics
Protozoan Proteins - physiology
Vacuoles - metabolism
Title PfCRT and the trans‐vacuolar proton electrochemical gradient: regulating the access of chloroquine to ferriprotoporphyrin IX
URI https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1365-2958.2006.05368.x
https://www.ncbi.nlm.nih.gov/pubmed/16956382
https://www.proquest.com/docview/196530652
https://search.proquest.com/docview/19536114
https://www.proquest.com/docview/68875581
https://pubmed.ncbi.nlm.nih.gov/PMC2943415
Volume 62
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