Erythrocyte binding antigen 175 (EBA-175)

Erythrocyte binding antigen 175 (EBA-175) is a 175 kDa micronemal protein expressed by the malaria parasite Plasmodium falciparum during its asexual blood stage [14, 17]. It serves as a critical adhesin that mediates the invasion of human erythrocytes by specifically binding to sialic acid residues on Glycophorin A, the most abundant glycoprotein on the red blood cell surface [1, 11, 12]. This interaction is essential for the formation of a tight junction between the merozoite and the host cell and triggers biophysical changes in the erythrocyte membrane, such as reducing its bending modulus, to facilitate parasite entry [3, 4, 20]. Due to its central role in the parasite life cycle and its ability to elicit neutralizing antibodies, EBA-175 is a leading candidate for blood-stage malaria vaccines [1, 13, 15]. Therapeutic development primarily targets the conserved Region II (RII) of the protein to induce antibodies that block the EBA-175-Glycophorin A interaction [13, 19]. However, the parasite's capacity to utilize redundant, sialic acid-independent invasion pathways and the presence of genetic polymorphisms pose significant challenges to the long-term efficacy of these interventions [2, 5, 18].

Other names

EBA175PfEBA-175Sialic acid-binding proteinEBP-1Erythrocyte-binding-like protein 1

Inhibition of parasite invasion into erythrocytes by blocking the interaction between EBA-175 and Glycophorin A and preventing parasite-host cell junction formation [1, 13, 19].