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
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.08.2016
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Summary: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.
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PMCID: PMC4958203
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.
ISSN:0066-4804
1098-6596
DOI:10.1128/AAC.03105-15