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

• Published in: Antimicrobial 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
• Language: English
• Published: United States American Society for Microbiology 01.08.2016
• Subjects: 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

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...