AustralieFrV1, Ncbi, Checkpoint, bibRecord, 002B41

Mutations in the Plasmodium falciparum chloroquine resistance transporter, PfCRT, enlarge the parasite’s food vacuole and alter drug sensitivities

Identifieur interne : 002B41 ( Ncbi/Checkpoint ); précédent : 002B40; suivant : 002B42

Mutations in the Plasmodium falciparum chloroquine resistance transporter, PfCRT, enlarge the parasite’s food vacuole and alter drug sensitivities

Auteurs : Serena Pulcini [Royaume-Uni] ; Henry M. Staines [Royaume-Uni] ; Andrew H. Lee [États-Unis] ; Sarah H. Shafik [Australie] ; Guillaume Bouyer [Royaume-Uni, France] ; Catherine M. Moore [Royaume-Uni] ; Daniel A. Daley [États-Unis] ; Matthew J. Hoke [États-Unis] ; Lindsey M. Altenhofen [États-Unis] ; Heather J. Painter [États-Unis] ; Jianbing Mu [États-Unis] ; David J. P. Ferguson [Royaume-Uni] ; Manuel Llinás [États-Unis] ; Rowena E. Martin [Australie] ; David A. Fidock [États-Unis] ; Roland A. Cooper [États-Unis] ; Sanjeev Krishna [Royaume-Uni]

Source :

Scientific Reports [ 2045-2322 ] ; 2015.

RBID : PMC:4588581

Descripteurs français

KwdFr :
- Animaux, Antipaludiques (pharmacologie), Chloroquine (pharmacologie), Humains, Mutation, Ovocytes (métabolisme), Plasmodium falciparum (), Plasmodium falciparum (physiologie), Protéines de protozoaire (), Protéines de protozoaire (génétique), Protéines de transport membranaire (), Protéines de transport membranaire (génétique), Résistance aux substances (génétique), Substitution d'acide aminé, Tests de sensibilité parasitaire, Transport biologique, Vacuoles (métabolisme), Xenopus laevis.
MESH :
- génétique : Protéines de protozoaire, Protéines de transport membranaire, Résistance aux substances.
- métabolisme : Ovocytes, Vacuoles.
- pharmacologie : Antipaludiques, Chloroquine.
- physiologie : Plasmodium falciparum.
- Animaux, Humains, Mutation, Plasmodium falciparum, Protéines de protozoaire, Protéines de transport membranaire, Substitution d'acide aminé, Tests de sensibilité parasitaire, Transport biologique, Xenopus laevis.

English descriptors

KwdEn :
- Amino Acid Substitution, Animals, Antimalarials (pharmacology), Biological Transport, Chloroquine (pharmacology), Drug Resistance (genetics), Humans, Membrane Transport Proteins (chemistry), Membrane Transport Proteins (genetics), Mutation, Oocytes (metabolism), Parasitic Sensitivity Tests, Plasmodium falciparum (drug effects), Plasmodium falciparum (physiology), Protozoan Proteins (chemistry), Protozoan Proteins (genetics), Vacuoles (metabolism), Xenopus laevis.
MESH :
- chemical , chemistry : Membrane Transport Proteins, Protozoan Proteins.
- chemical , genetics : Membrane Transport Proteins, Protozoan Proteins.
- chemical , pharmacology : Antimalarials, Chloroquine.
- drug effects : Plasmodium falciparum.
- genetics : Drug Resistance.
- metabolism : Oocytes, Vacuoles.
- physiology : Plasmodium falciparum.
- Amino Acid Substitution, Animals, Biological Transport, Humans, Mutation, Parasitic Sensitivity Tests, Xenopus laevis.

Abstract

Mutations in the Plasmodium falciparum chloroquine resistance transporter, PfCRT, are the major determinant of chloroquine resistance in this lethal human malaria parasite. Here, we describe P. falciparum lines subjected to selection by amantadine or blasticidin that carry PfCRT mutations (C101F or L272F), causing the development of enlarged food vacuoles. These parasites also have increased sensitivity to chloroquine and some other quinoline antimalarials, but exhibit no or minimal change in sensitivity to artemisinins, when compared with parental strains. A transgenic parasite line expressing the L272F variant of PfCRT confirmed this increased chloroquine sensitivity and enlarged food vacuole phenotype. Furthermore, the introduction of the C101F or L272F mutation into a chloroquine-resistant variant of PfCRT reduced the ability of this protein to transport chloroquine by approximately 93 and 82%, respectively, when expressed in Xenopus oocytes. These data provide, at least in part, a mechanistic explanation for the increased sensitivity of the mutant parasite lines to chloroquine. Taken together, these findings provide new insights into PfCRT function and PfCRT-mediated drug resistance, as well as the food vacuole, which is an important target of many antimalarial drugs.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4588581

DOI: 10.1038/srep14552
PubMed: 26420308
PubMed Central: 4588581

Affiliations:

Australie, France, Royaume-Uni, États-Unis

Links to Exploration step

PMC:4588581

Le document en format XML

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 chloroquine resistance transporter, PfCRT, enlarge the parasite’s food vacuole and alter drug sensitivities</title>
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<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Mutations in the <italic>Plasmodium falciparum</italic>
 chloroquine resistance transporter, PfCRT, enlarge the parasite’s food vacuole and alter drug sensitivities</title>
<author><name sortKey="Pulcini, Serena" sort="Pulcini, Serena" uniqKey="Pulcini S" first="Serena" last="Pulcini">Serena Pulcini</name>
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, London SW17 0RE,<country>UK</country>
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, Rockville MD 20852,<country>USA</country>
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<country xml:lang="fr">États-Unis</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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, Oxford OX3 9DU,<country>UK</country>
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<country xml:lang="fr">Royaume-Uni</country>
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<author><name sortKey="Llinas, Manuel" sort="Llinas, Manuel" uniqKey="Llinas M" first="Manuel" last="Llinás">Manuel Llinás</name>
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, Pennsylvania 16802,<country>USA</country>
</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Martin, Rowena E" sort="Martin, Rowena E" uniqKey="Martin R" first="Rowena E." last="Martin">Rowena E. Martin</name>
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, Canberra, ACT 2601,<country>Australia</country>
</nlm:aff>
<country xml:lang="fr">Australie</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Fidock, David A" sort="Fidock, David A" uniqKey="Fidock D" first="David A." last="Fidock">David A. Fidock</name>
<affiliation wicri:level="1"><nlm:aff id="a2"><institution>Department of Microbiology and Immunology, Columbia University Medical Center</institution>
, New York, NY 10032,<country>USA</country>
</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="a10"><institution>Division of Infectious Diseases, Department of Medicine, Columbia University Medical Center</institution>
, New York, NY 10032,<country>USA</country>
</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Cooper, Roland A" sort="Cooper, Roland A" uniqKey="Cooper R" first="Roland A." last="Cooper">Roland A. Cooper</name>
<affiliation wicri:level="1"><nlm:aff id="a6"><institution>Department of Biological Sciences, Old Dominion University</institution>
, Norfolk, VA 23529,<country>USA</country>
</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="a11"><institution>Department of Natural Sciences and Mathematics, Dominican University of California</institution>
, San Rafael, CA 94901,<country>USA</country>
</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Krishna, Sanjeev" sort="Krishna, Sanjeev" uniqKey="Krishna S" first="Sanjeev" last="Krishna">Sanjeev Krishna</name>
<affiliation wicri:level="1"><nlm:aff id="a1"><institution>Institute for Infection and Immunity, St. George’s, University of London</institution>
, London SW17 0RE,<country>UK</country>
</nlm:aff>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
</analytic>
<series><title level="j">Scientific Reports</title>
<idno type="eISSN">2045-2322</idno>
<imprint><date when="2015">2015</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term>
<term>Animals</term>
<term>Antimalarials (pharmacology)</term>
<term>Biological Transport</term>
<term>Chloroquine (pharmacology)</term>
<term>Drug Resistance (genetics)</term>
<term>Humans</term>
<term>Membrane Transport Proteins (chemistry)</term>
<term>Membrane Transport Proteins (genetics)</term>
<term>Mutation</term>
<term>Oocytes (metabolism)</term>
<term>Parasitic Sensitivity Tests</term>
<term>Plasmodium falciparum (drug effects)</term>
<term>Plasmodium falciparum (physiology)</term>
<term>Protozoan Proteins (chemistry)</term>
<term>Protozoan Proteins (genetics)</term>
<term>Vacuoles (metabolism)</term>
<term>Xenopus laevis</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Antipaludiques (pharmacologie)</term>
<term>Chloroquine (pharmacologie)</term>
<term>Humains</term>
<term>Mutation</term>
<term>Ovocytes (métabolisme)</term>
<term>Plasmodium falciparum ()</term>
<term>Plasmodium falciparum (physiologie)</term>
<term>Protéines de protozoaire ()</term>
<term>Protéines de protozoaire (génétique)</term>
<term>Protéines de transport membranaire ()</term>
<term>Protéines de transport membranaire (génétique)</term>
<term>Résistance aux substances (génétique)</term>
<term>Substitution d'acide aminé</term>
<term>Tests de sensibilité parasitaire</term>
<term>Transport biologique</term>
<term>Vacuoles (métabolisme)</term>
<term>Xenopus laevis</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Transport Proteins</term>
<term>Protozoan Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Transport Proteins</term>
<term>Protozoan Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antimalarials</term>
<term>Chloroquine</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Drug Resistance</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de protozoaire</term>
<term>Protéines de transport membranaire</term>
<term>Résistance aux substances</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Oocytes</term>
<term>Vacuoles</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Ovocytes</term>
<term>Vacuoles</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antipaludiques</term>
<term>Chloroquine</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term>
<term>Animals</term>
<term>Biological Transport</term>
<term>Humans</term>
<term>Mutation</term>
<term>Parasitic Sensitivity Tests</term>
<term>Xenopus laevis</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Humains</term>
<term>Mutation</term>
<term>Plasmodium falciparum</term>
<term>Protéines de protozoaire</term>
<term>Protéines de transport membranaire</term>
<term>Substitution d'acide aminé</term>
<term>Tests de sensibilité parasitaire</term>
<term>Transport biologique</term>
<term>Xenopus laevis</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>Mutations in the <italic>Plasmodium falciparum</italic>
 chloroquine resistance transporter, PfCRT, are the major determinant of chloroquine resistance in this lethal human malaria parasite. Here, we describe <italic>P. falciparum</italic>
 lines subjected to selection by amantadine or blasticidin that carry PfCRT mutations (C101F or L272F), causing the development of enlarged food vacuoles. These parasites also have increased sensitivity to chloroquine and some other quinoline antimalarials, but exhibit no or minimal change in sensitivity to artemisinins, when compared with parental strains. A transgenic parasite line expressing the L272F variant of PfCRT confirmed this increased chloroquine sensitivity and enlarged food vacuole phenotype. Furthermore, the introduction of the C101F or L272F mutation into a chloroquine-resistant variant of PfCRT reduced the ability of this protein to transport chloroquine by approximately 93 and 82%, respectively, when expressed in Xenopus oocytes. These data provide, at least in part, a mechanistic explanation for the increased sensitivity of the mutant parasite lines to chloroquine. Taken together, these findings provide new insights into PfCRT function and PfCRT-mediated drug resistance, as well as the food vacuole, which is an important target of many antimalarial drugs.</p>
</div>
</front>
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<name sortKey="Painter, Heather J" sort="Painter, Heather J" uniqKey="Painter H" first="Heather J." last="Painter">Heather J. Painter</name>
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<name sortKey="Martin, Rowena E" sort="Martin, Rowena E" uniqKey="Martin R" first="Rowena E." last="Martin">Rowena E. Martin</name>
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   |texte=   Mutations in the Plasmodium falciparum chloroquine resistance transporter, PfCRT, enlarge the parasite’s food vacuole and alter drug sensitivities
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Serveur d'exploration sur les relations entre la France et l'Australie

Mutations in the Plasmodium falciparum chloroquine resistance transporter, PfCRT, enlarge the parasite’s food vacuole and alter drug sensitivities

Mutations in the Plasmodium falciparum chloroquine resistance transporter, PfCRT, enlarge the parasite’s food vacuole and alter drug sensitivities

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	Serveur d'exploration sur les relations entre la France et l'Australie
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