Open AccessAbsence 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
Author(s) -
Mathieu Gendrot,
Bécaye Fall,
Marylin Madamet,
Mansour Fall,
Khalifa Ababacar Wade,
Rémy Amalvict,
Aminata Nakoulima,
Nicolas Benoît,
Silman Diawara,
Yaya Diémé,
Bakary Diatta,
Boubacar Wade,
Bruno Pradines
Publication year - 2016
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.03105-15
Subject(s) - ubiquitin ligase , biology , plasmodium falciparum , ubiquitin , gene , genetics , dna ligase , mutation , ex vivo , piperaquine , microbiology and biotechnology , in vivo , malaria , immunology , artemisinin
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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