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

The Plasmodium falciparum reticulocyte-binding protein homolog 5 (PfRH5) – human basigin (BSG/CD147) interface is a critical protein-protein interaction required for the invasion of human erythrocytes by the malaria parasite. PfRH5 is a highly conserved, essential secreted protein that forms a larger complex with other parasite proteins (CyRPA and RIPR) to facilitate host cell entry. Unlike many other parasite invasion ligands, PfRH5 is indispensable across all known strains of P. falciparum, making it a premier target for blood-stage malaria vaccines and therapeutic antibodies. The interaction occurs when PfRH5 binds to the distal immunoglobulin domain of Basigin on the red blood cell surface, triggering the formation of a tight junction and subsequent parasite entry. Therapeutic strategies focus on developing vaccines, such as RH5.1, or monoclonal antibodies that sterically hinder this binding event to neutralize the parasite before it can establish an intracellular infection. Because this interface is the only known essential pathway for P. falciparum invasion that is not redundant, it represents a high-priority target for achieving long-term immunity against malaria.

Other names

PfRH5-CD147 complexRH5-Basigin interactionMerozoite surface protein RH5-Basigin interfacePfRH5-BSG protein-protein interface

Inhibition of protein-protein interaction, Neutralization of parasite invasion, Blocking erythrocyte binding