TY - JOUR
T1 - Ion Regulation in the Malaria Parasite
AU - Kirk, Kiaran
N1 - Publisher Copyright:
Copyright ©2015 by Annual Reviews. All rights reserved.
PY - 2015/10/15
Y1 - 2015/10/15
N2 - Some hours after invading the erythrocytes of its human host, the malaria parasite Plasmodium falciparum induces an increase in the permeability of the erythrocyte membrane to monovalent ions. The resulting net influx of Na+ and net efflux of K+, down their respective concentration gradients, converts the erythrocyte cytosol from an initially high-K+, low-Na+ solution to a high-Na+, low-K+ solution. The intraerythrocytic parasite itself exerts tight control over its internal Na+, K+, Cl-, and Ca2+ concentrations and its intracellular pH through the combined actions of a range of membrane transport proteins. The molecular mechanisms underpinning ion regulation in the parasite are receiving increasing attention, not least because PfATP4, a P-type ATPase postulated to be involved in Na+ regulation, has emerged as a potential antimalarial drug target, susceptible to inhibition by a wide range of chemically unrelated compounds.
AB - Some hours after invading the erythrocytes of its human host, the malaria parasite Plasmodium falciparum induces an increase in the permeability of the erythrocyte membrane to monovalent ions. The resulting net influx of Na+ and net efflux of K+, down their respective concentration gradients, converts the erythrocyte cytosol from an initially high-K+, low-Na+ solution to a high-Na+, low-K+ solution. The intraerythrocytic parasite itself exerts tight control over its internal Na+, K+, Cl-, and Ca2+ concentrations and its intracellular pH through the combined actions of a range of membrane transport proteins. The molecular mechanisms underpinning ion regulation in the parasite are receiving increasing attention, not least because PfATP4, a P-type ATPase postulated to be involved in Na+ regulation, has emerged as a potential antimalarial drug target, susceptible to inhibition by a wide range of chemically unrelated compounds.
KW - Channel
KW - Membrane transport
KW - PfATP4
KW - Plasmodium
KW - Pump
KW - Transporter
UR - http://www.scopus.com/inward/record.url?scp=84945261954&partnerID=8YFLogxK
U2 - 10.1146/annurev-micro-091014-104506
DO - 10.1146/annurev-micro-091014-104506
M3 - Review article
SN - 0066-4227
VL - 69
SP - 341
EP - 359
JO - Annual Review of Microbiology
JF - Annual Review of Microbiology
IS - 1
ER -