Reticulocyte-binding protein homolog 5-interacting protein (Ripr) (Ripr)

RH5-interacting protein (Ripr) is a critical component of the Plasmodium falciparum invasion machinery, forming a stable ternary complex with Reticulocyte-binding protein homolog 5 (RH5) and Cysteine-rich protective antigen (CyRPA) (Wong et al., 2019, Nature). This complex is essential for the parasite's ability to invade human erythrocytes, a key step in the malaria life cycle (Chen et al., 2011, Proc Natl Acad Sci USA). Ripr is a large, 126-kDa cysteine-rich protein localized to the micronemes of the merozoite and is released onto the parasite surface during the invasion process (Healer et al., 2019, Infect Immun). Because the RH5-CyRPA-Ripr complex is indispensable for blood-stage infection and is relatively conserved across different strains of P. falciparum, Ripr has emerged as a high-priority target for malaria vaccine development and monoclonal antibody therapies (Ragotte et al., 2020, Cell Host Microbe). Neutralizing antibodies against Ripr have been shown to effectively block erythrocyte invasion in vitro and provide protection in animal models (Draper et al., 2018, Cell Host Microbe). Current therapeutic strategies focus on inducing potent inhibitory antibodies that disrupt the assembly or function of the invasion complex to prevent clinical malaria (Nilsen et al., 2023, NPJ Vaccines).

Other names

PfRiprRH5-interacting proteinPlasmodium falciparum RH5-interacting proteinP. falciparum Ripr

Inhibition of erythrocyte invasion by blocking the formation or function of the RH5-CyRPA-Ripr complex, thereby preventing the parasite from entering host red blood cells.