Erythrocyte-binding antigen 175 (EBA-175) (EBA-175)

Erythrocyte-binding antigen 175 (EBA-175) is a critical 175-kDa ligand expressed by the merozoite stage of Plasmodium falciparum, the most lethal human malaria parasite [1, 12]. Region II (RII) of EBA-175 is the functional domain composed of two cysteine-rich Duffy-binding-like (DBL) domains, F1 and F2, which specifically recognize and bind to sialic acid residues on Glycophorin A (GPA) on the human erythrocyte surface [7, 9]. This binding event is a prerequisite for the formation of a tight junction and subsequent invasion of the red blood cell [13]. Beyond simple attachment, the EBA-175/GPA interaction triggers a phosphorylation cascade that alters the biophysical deformability of the host cell membrane, facilitating parasite entry [8, 10]. As a primary mediator of the sialic acid-dependent invasion pathway, EBA-175 RII is a leading target for blood-stage malaria vaccines and inhibitory monoclonal antibodies [3, 4]. Clinical trials have evaluated recombinant non-glycosylated EBA-175 RII (EBA-175 RII-NG) as a vaccine candidate, demonstrating safety and the induction of growth-inhibitory antibodies [5, 6]. However, the existence of alternative, sialic acid-independent invasion pathways and antigenic variation among different parasite strains present significant challenges for the development of universally effective therapeutics targeting this domain [2, 14].

Other names

EBA175Erythrocyte-binding proteinPfEBA-175Region II of EBA-175EBA-175 RII

Blocking the interaction between the parasite's EBA-175 Region II and the host's Glycophorin A receptor to prevent erythrocyte invasion and subsequent parasite replication.