Plasmodium falciparum Cysteine-rich protective antigen (CyRPA) (CyRPA)

Cysteine-rich protective antigen (CyRPA) is a 30-kDa protein essential for the invasion of human erythrocytes by Plasmodium falciparum (UniProt Q8I6R7). It forms a critical tripartite complex with Reticulocyte-binding protein homolog 5 (Rh5) and Rh5-interacting protein (Ripr), known as the RCR complex (Chen et al., 2017, Nature). CyRPA acts as a scaffold that facilitates the assembly of this complex, which is required for the parasite to enter red blood cells and cause malaria (Ragotte et al., 2020, Cell Reports). Because CyRPA is highly conserved and lacks significant genetic polymorphism, it is a primary target for blood-stage malaria vaccines and monoclonal antibody therapies (Favuzza et al., 2020, Cell Host & Microbe). Neutralizing antibodies targeting specific CyRPA epitopes can block the formation of the RCR complex or its function, effectively preventing parasite replication. Therapeutic development focuses on identifying the most potent epitopes to elicit a robust and durable immune response in at-risk populations.

Other names

CyRPAPF3D7_0423800Cysteine-rich protective antigenP. falciparum CyRPACyRPA epitopes

Neutralizing antibodies bind to specific epitopes on CyRPA, disrupting the formation or stability of the Rh5-CyRPA-Ripr (RCR) complex, which is essential for the invasion of human red blood cells by Plasmodium falciparum merozoites.