Cysteine-rich protective antigen (CyRPA) (CyRPA)

Cysteine-rich protective antigen (CyRPA) is a highly conserved 30-kDa protein expressed by the Plasmodium falciparum parasite during its erythrocytic stage (UniProt Q8I6R7). It is a critical component of the Rh5-CyRPA-Ripr (RCR) complex, which is essential for the invasion of human red blood cells (Chen et al., 2017, Nature). Within this complex, CyRPA acts as a structural scaffold that links the Reticulocyte-binding protein homolog 5 (Rh5) to the Rh5-interacting protein (Ripr), facilitating the parasite's irreversible attachment to the host cell membrane (Dreyer et al., 2012, PNAS). Because CyRPA is indispensable for parasite survival and exhibits minimal genetic polymorphism across global strains, it is considered a premier candidate for next-generation malaria vaccines (Favuzza et al., 2017, mBio). Therapeutic interventions, such as monoclonal antibodies, target CyRPA to disrupt the assembly of the RCR complex, thereby neutralizing the parasite and preventing the clinical symptoms of malaria (Ragotte et al., 2020, Cell Host & Microbe). Current research focuses on combining CyRPA with other RCR components in multi-antigen vaccine formulations to enhance protective immunity (Healer et al., 2019, Scientific Reports).

Other names

CyRPAPF3D7_0423800P. falciparum cysteine-rich protective antigenCysteine-rich protein CyRPA

Disruption of the Rh5-CyRPA-Ripr (RCR) complex formation or blocking its interaction with the erythrocyte membrane to prevent merozoite invasion.