Effects of G6PD deficiency on the phosphorylation and carbonylation of membrane protein complexes of human erythrocytes infected with Plasmodium falciparum

ABSTRACT: The ancestral parasite-host relationship associated with human malaria has driven the emergence of mutations in genes, such as erythrocyte glucose-6-phosphate dehydrogenase (G6PD), that confer resistance to lethal malaria and enhance human survival. Protein complexes in the erythrocyte membrane play a crucial role in maintaining red blood cell integrity and elasticity, both of which are essential for the parasite’s asexual life cycle. To facilitate this, the Plasmodium falciparum parasite exports proteins that interact with erythrocyte membrane proteins on the cell surface. However, how G6PD deficiency affects the Plasmodium exportome, and the potential role of post-translational modifications (PTMs), such as phosphorylation, direct carbonylation, and 4-hydroxynonenal (4-HNE) carbonylation, on host cell membrane proteins in this interaction remain largely unexplored

INSTRUMENT(S):

ORGANISM(S): Plasmodium Falciparum Homo Sapiens (human)

TISSUE(S): Erythrocyte, Blood

DISEASE(S): Malaria,Glucosephosphate Dehydrogenase Deficiency

SUBMITTER: Concha Gil  

LAB HEAD: Darío Méndez Cuadro

PROVIDER: PXD061301 | Pride | 2026-09-28

REPOSITORIES: Pride