Plasmodium falciparum reticulocyte-binding protein homolog 5 (PfRH5)

Plasmodium falciparum reticulocyte-binding protein homolog 5 (PfRH5) is an essential, highly conserved parasite protein critical for the invasion of human erythrocytes by P. falciparum, the most virulent malaria species. Unlike other members of the reticulocyte-binding homolog (RH) family, PfRH5 is smaller, lacking certain transmembrane/cytosolic features, and functions as part of a protein complex (PCRCR or RCR) with CyRPA, RIPR, and TRAMP proteins. PfRH5 binds to the human erythrocyte receptor basigin (CD147), an interaction universally required for parasite invasion. This makes it a leading target for vaccines and monoclonal antibodies aiming to block parasite entry, with clinical development in progress. Targeting PfRH5 has shown to confer robust, strain-transcending protective immunity in vitro and in vivo, with identified potent human antibody clonotypes serving both as candidate therapeutics and biomarkers for protection[2][3][4][6][7]. Polymorphism in the basigin binding site and immune escape are considered when designing next-generation interventions.

Other names

RH5Reticulocyte-binding protein homolog 5PfRH5 protein

Inhibition of erythrocyte invasion by neutralizing antibody (for vaccine/antibody); Potential small-molecule disruption of receptor binding