Plasmodium vivax mitochondrial and cytosolic redox systems (Pv Redox Systems)

The Plasmodium vivax mitochondrial and cytosolic redox systems comprise a complex network of enzymes and molecules dedicated to maintaining the parasite's intracellular reduction-oxidation balance. In the cytosol, the thioredoxin and glutathione systems are the primary defenses against oxidative damage caused by the host's immune response and the parasite's own metabolism, particularly the release of toxic heme during hemoglobin degradation (Sarma et al., 2021). The mitochondrial redox system is centered around the electron transport chain, which is essential not only for ATP production but also for providing electrons to dihydroorotate dehydrogenase, a key enzyme in pyrimidine biosynthesis (Biagini et al., 2006). These systems are critical therapeutic targets because P. vivax is highly sensitive to oxidative stress and lacks certain redundant antioxidant pathways found in humans, such as catalase (Müller et al., 2017). Drugs like atovaquone target the mitochondrial cytochrome bc1 complex, while 8-aminoquinolines like primaquine and tafenoquine are believed to interfere with redox homeostasis, specifically to eliminate dormant liver-stage hypnozoites (Ashley et al., 2018). Because these pathways are distinct from host systems or essential for parasite survival in unique ways, they offer a significant therapeutic window for antimalarial intervention. However, targeting these systems requires careful consideration of host safety, as drugs that induce oxidative stress can cause severe hemolysis in individuals with glucose-6-phosphate dehydrogenase (G6PD) deficiency.

Other names

P. vivax redox metabolismPlasmodium vivax antioxidant systemsPv mitochondrial and cytosolic antioxidant network

Inhibition of mitochondrial electron transport or cytosolic antioxidant enzymes (thioredoxin/glutathione reductases) to induce lethal oxidative stress and metabolic arrest.