Plasmodium falciparum reticulocyte-binding protein homolog 5 – basigin interface (PfRH5-BSG interface)

The Plasmodium falciparum reticulocyte-binding protein homolog 5 (PfRH5) – basigin interface is a critical point of contact required for the invasion of human erythrocytes by the malaria parasite (Wright et al., 2014, Nature). PfRH5 is a highly conserved parasite protein that forms a complex with other proteins, including CyRPA and RIPR, and binds to the human receptor basigin (also known as CD147) on the red blood cell surface (Crosnier et al., 2011, Nature). This interaction is essential for all known strains of P. falciparum, making it a premier target for blood-stage malaria vaccines and therapeutic antibodies (Douglas et al., 2011, Nature Communications). Unlike many other parasite surface proteins, PfRH5 shows limited genetic polymorphism, which reduces the likelihood of strain-specific immunity and makes it an attractive candidate for a universal vaccine (Bustamante et al., 2013, Vaccine). Therapeutic strategies focus on developing monoclonal antibodies or vaccines, such as the RH5.1 candidate, that induce neutralizing antibodies to sterically hinder this binding event (Minassian et al., 2021, Science Translational Medicine). Successful blockade of this interface prevents the parasite from entering the host cell, thereby halting the asexual replication cycle responsible for the clinical symptoms and pathology of malaria.

Other names

PfRH5-CD147 interfaceRH5-Basigin complexReticulocyte-binding protein homolog 5 – basigin interaction

Blocking the essential interaction between the parasite protein PfRH5 and the human erythrocyte receptor Basigin to prevent Plasmodium falciparum from invading red blood cells.