Results of cryo-electron microscopy (cryo-EM) studies revealed the molecular mechanism by which the Plasmodium vivax malaria parasite binds to and invades red blood cells in the human host.
TfR1-deficient erythroid cells were refractory to invasion by P. vivax, and anti-PvRBP2b (P. vivax reticulocyte-binding protein 2b) monoclonal antibodies inhibited reticulocyte binding and blocked P. vivax invasion in field isolates.P. vivax is one of the five species of malaria parasites that commonly infect humans. Plasmodium vivax is a protozoal parasite and a human pathogen.
Although it is less virulent than Plasmodium falciparum, the deadliest of the five human malaria parasites, P. vivax malaria infections can lead to severe disease and death.However, latest studies have indicated that human P. vivax is actually of African origin. Functional analyses of TfR1 highlighted how P. vivax hijacked TfR1, an essential housekeeping protein, by binding to sites that govern host specificity, without affecting its cellular function of transporting iron.
vivax parasites are incredibly diverse – which is challenging for vaccine development. “With this unprecedented level of detail, we can now begin to design new therapies that specifically target and disrupt the parasite’s invasion machinery, preventing malaria parasites from hijacking human red blood cells to spread through the blood and, ultimately, be transmitted to others.”