title: Ion and nutrient uptake by malaria parasite-infected erythrocytes.
abstract: Erythrocytes infected with malaria parasites have increased permeability to diverse organic and inorganic solutes. While these permeability changes have been known for decades, the molecular basis of transport was unknown and intensively debated. CLAG3, a parasite protein previously thought to function in cytoadherence, has recently been implicated in formation of the plasmodial surface anion channel (PSAC), an unusual small conductance ion channel that mediates uptake of most solutes. Consistent with transport studies, the clag genes are conserved in all plasmodia but are absent from other genera. The encoded protein is integral to the host membrane, as also predicted by electrophysiology. An important question is whether functional channels are formed by CLAG3 alone or through interactions with other proteins. In either case, gene identification should advance our understanding of parasite biology and may lead to new therapeutics.
authors.affiliation: The Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20894, USA. sdesai@niaid.nih.gov
authors.forename: Sanjay A
authors.initials: SA
authors.lastname: Desai
mesh_terms: D000818:Animals; D004912:Erythrocytes / Q000378:metabolism* / Q000469:parasitology*; D006801:Humans; D007287:Inorganic Chemicals / Q000378:metabolism*; D007477:Ions / Q000378:metabolism*; D008288:Malaria / Q000469:parasitology / Q000503:physiopathology*; D009930:Organic Chemicals / Q000378:metabolism*; D010961:Plasmodium / Q000378:metabolism / Q000472:pathogenicity*; D015800:Protozoan Proteins / Q000378:metabolism
chemical_list: D007287:Inorganic Chemicals; D007477:Ions; D009930:Organic Chemicals; D015800:Protozoan Proteins; C502072:cytoadherence-linked asexual protein 3, Plasmodium falciparum