Abstract
Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common enzymatic disorder in humans and appears to be protective against falciparum severe malaria. Controversially, it is also thought that Plasmodium vivax has driven the recent selection of G6PD alleles. We use an experimental approach to determine whether G6PD-MahidolG487A variant, a widespread cause of severe G6PD deficiency in Southeast Asia, provides a barrier against vivax malaria. Our results show that the immature reticulocytes (CD71+) targeted by P. vivax invasion are enzymatically normal, even in hemizygous G6PD-Mahidol G487A mutants; thus, allowing the normal growth, development, and high parasite density in severely deficient samples.
Highlights
Mutations in the X-linked glucose-6-phosphate dehydrogenase (G6PD) gene are the most common and widespread cause of human enzymopathy; they are associated with stress-induced hemolysis, resulting in a range of mild to life-threatening clinical conditions
P. vivax targets a specific population of immature reticulocytes (CD71+), which are primarily found in the bone marrow [12]
Our hypothesis was that selection of G6PD mutations by P. vivax might be mediated by phenotypic deficiency in those young reticulocytes, whereby the parasite would be unable to invade or normally replicate in red blood cells (RBCs) whose intracellular capacity of respond to stress was decreased by lack of G6PD activity
Summary
Mutations in the X-linked glucose-6-phosphate dehydrogenase (G6PD) gene are the most common and widespread cause of human enzymopathy; they are associated with stress-induced hemolysis, resulting in a range of mild to life-threatening clinical conditions. Blood samples were collected at the Thailand–Myanmar border among subjects of Karen ethnicity where the prevalence of G6PD can reach 15%; the major variant found in the population is Mahidol (487G>A) (Supplementary Figure 1).
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