Erythrocyte-binding antigen 175 - Glycophorin A interaction (EBA-175 - GYPA interaction)

The interaction between Erythrocyte-binding antigen 175 (EBA-175) and Glycophorin A (GYPA) is a fundamental molecular event in the pathogenesis of Plasmodium falciparum malaria (Tolia et al., 2005, PubMed: 16015336). EBA-175 is a parasite-produced ligand that utilizes its Region II (RII) domain to specifically recognize and bind to the sialic acid residues on the extracellular domain of Glycophorin A, the most abundant sialoglycoprotein on the human erythrocyte surface (Sim et al., 1994, PubMed: 8139654). This binding event is a key component of the sialic acid-dependent invasion pathway, facilitating the formation of a tight junction between the parasite merozoite and the host cell, which is essential for successful entry (Orlandi et al., 1992, PubMed: 1311054). Because this interaction represents a critical bottleneck in the parasite's life cycle, it is a primary target for the development of blood-stage malaria vaccines and inhibitory monoclonal antibodies (Healer et al., 2013, PubMed: 23515247). Therapeutic strategies focus on blocking this protein-protein interaction to prevent erythrocyte infection and reduce clinical disease severity. However, the parasite's ability to utilize alternative, sialic acid-independent invasion pathways and the presence of genetic polymorphisms in EBA-175 present significant challenges for long-term drug and vaccine efficacy (Ambroggio et al., 2013, PubMed: 23408601).

Other names

EBA-175 RII - Glycophorin A complexPfEBA-175 - GYPA interactionSialic acid-dependent invasion pathwayErythrocyte-binding antigen 175 region II - Glycophorin A interaction

Inhibition of the binding between EBA-175 and Glycophorin A to prevent Plasmodium falciparum merozoite invasion of erythrocytes (Tolia et al., 2005).