Absence of Association between Polymorphisms in the RING E3 Ubiquitin Protein Ligase Gene and Ex Vivo Susceptibility to Conventional Antimalarial Drugs in Plasmodium falciparum Isolates from Dakar, Senegal

The RING E3 ubiquitin protein ligase is crucial for facilitating the transfer of ubiquitin. The only polymorphism identified in the E3 ubiquitin protein ligase gene was the D113N mutation (62.5%) but was not significantly associated with the 50% inhibitory concentration (IC50) of conventional antima...

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Published inAntimicrobial agents and chemotherapy Vol. 60; no. 8; pp. 5010 - 5013
Main Authors Gendrot, Mathieu, Fall, Bécaye, Madamet, Marylin, Fall, Mansour, Wade, Khalifa Ababacar, Amalvict, Rémy, Nakoulima, Aminata, Benoit, Nicolas, Diawara, Silman, Diémé, Yaya, Diatta, Bakary, Wade, Boubacar, Pradines, Bruno
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LanguageEnglish
Published United States American Society for Microbiology 01.08.2016
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Abstract The RING E3 ubiquitin protein ligase is crucial for facilitating the transfer of ubiquitin. The only polymorphism identified in the E3 ubiquitin protein ligase gene was the D113N mutation (62.5%) but was not significantly associated with the 50% inhibitory concentration (IC50) of conventional antimalarial drugs. However, some mutated isolates (D113N) present a trend of reduced susceptibility to piperaquine (P = 0.0938). To evaluate the association of D113N polymorphism with susceptibility to antimalarials, more isolates are necessary.
AbstractList The RING E3 ubiquitin protein ligase is crucial for facilitating the transfer of ubiquitin. The only polymorphism identified in the E3 ubiquitin protein ligase gene was the D113N mutation (62.5%) but was not significantly associated with the 50% inhibitory concentration (IC50) of conventional antimalarial drugs. However, some mutated isolates (D113N) present a trend of reduced susceptibility to piperaquine (P = 0.0938). To evaluate the association of D113N polymorphism with susceptibility to antimalarials, more isolates are necessary.
ABSTRACT The RING E3 ubiquitin protein ligase is crucial for facilitating the transfer of ubiquitin. The only polymorphism identified in the E3 ubiquitin protein ligase gene was the D113N mutation (62.5%) but was not significantly associated with the 50% inhibitory concentration (IC 50 ) of conventional antimalarial drugs. However, some mutated isolates (D113N) present a trend of reduced susceptibility to piperaquine ( P = 0.0938). To evaluate the association of D113N polymorphism with susceptibility to antimalarials, more isolates are necessary.
The RING E3 ubiquitin protein ligase is crucial for facilitating the transfer of ubiquitin. The only polymorphism identified in the E3 ubiquitin protein ligase gene was the D113N mutation (62.5%) but was not significantly associated with the 50% inhibitory concentration (IC 50 ) of conventional antimalarial drugs. However, some mutated isolates (D113N) present a trend of reduced susceptibility to piperaquine ( P = 0.0938). To evaluate the association of D113N polymorphism with susceptibility to antimalarials, more isolates are necessary.
Author Wade, Boubacar
Nakoulima, Aminata
Wade, Khalifa Ababacar
Diatta, Bakary
Benoit, Nicolas
Madamet, Marylin
Fall, Mansour
Amalvict, Rémy
Fall, Bécaye
Diémé, Yaya
Gendrot, Mathieu
Diawara, Silman
Pradines, Bruno
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  organization: Unité de Parasitologie et d'Entomologie, Département des Maladies Infectieuses, Institut de Recherche Biomédicale des Armées, Brétigny sur Orge, France Aix Marseille Université, Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes, UM 63, CNRS 7278, IRD 198, Inserm 1095, Marseille, France Laboratoire d'étude de la chimiosensibilité du paludisme, Fédération des laboratoires, Hôpital Principal de Dakar, Dakar, Sénégal Centre national de référence du Paludisme, Marseille, France bruno.pradines@free.fr
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Copyright © 2016, American Society for Microbiology. All Rights Reserved. 2016 American Society for Microbiology
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Citation Gendrot M, Fall B, Madamet M, Fall M, Wade KA, Amalvict R, Nakoulima A, Benoit N, Diawara S, Diémé Y, Diatta B, Wade B, Pradines B. 2016. Absence of association between polymorphisms in the RING E3 ubiquitin protein ligase gene and ex vivo susceptibility to conventional antimalarial drugs in Plasmodium falciparum isolates from Dakar, Senegal. Antimicrob Agents Chemother 60:5010–5013. doi:10.1128/AAC.03105-15.
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Snippet The RING E3 ubiquitin protein ligase is crucial for facilitating the transfer of ubiquitin. The only polymorphism identified in the E3 ubiquitin protein ligase...
ABSTRACT The RING E3 ubiquitin protein ligase is crucial for facilitating the transfer of ubiquitin. The only polymorphism identified in the E3 ubiquitin...
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SubjectTerms Antimalarials
Antimalarials - pharmacology
Artemisinins - pharmacology
Chloroquine - analogs & derivatives
Chloroquine - pharmacology
Doxycycline - pharmacology
Ethanolamines - pharmacology
Fluorenes - pharmacology
Human health and pathology
Infectious diseases
Life Sciences
Mechanisms of Resistance
Mefloquine - pharmacology
Naphthyridines - pharmacology
Plasmodium falciparum
Plasmodium falciparum - drug effects
Plasmodium falciparum - genetics
Polymorphism, Genetic
Polymorphism, Genetic - genetics
Quinine - pharmacology
Quinolines - pharmacology
Senegal
Ubiquitin-Protein Ligases
Ubiquitin-Protein Ligases - genetics
Title Absence of Association between Polymorphisms in the RING E3 Ubiquitin Protein Ligase Gene and Ex Vivo Susceptibility to Conventional Antimalarial Drugs in Plasmodium falciparum Isolates from Dakar, Senegal
URI https://www.ncbi.nlm.nih.gov/pubmed/27185795
https://journals.asm.org/doi/10.1128/AAC.03105-15
https://search.proquest.com/docview/1807080785
https://search.proquest.com/docview/1811881748
https://hal.science/hal-01455596
https://pubmed.ncbi.nlm.nih.gov/PMC4958203
Volume 60
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