Erythrocyte invasion by malaria parasites is mediated by specific molecular interactions.
Sialic acid residues of glycophorin A are used as invasion receptors by Plasmodium …

The ligands that pathogens use to invade their target cells have often proven to be good
targets for vaccine development. However, Plasmodium falciparum has redundant ligands …

The 175-kDa Plasmodium falciparum erythrocyte binding protein (EBA-175) binds to its
receptor, sialic acids on glycophorin A. The binding region within EBA-175 is a cysteine-rich …

The Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175) is a ligand for
merozoite invasion into human erythrocytes that binds to glycophorin A in a sialic acid …

In vitro experimentation with Plasmodium falciparum has determined that a number of
different receptor-ligand interactions are involved in the invasion of erythrocytes. Most …

Erythrocyte invasion by Plasmodium requires molecules present both on the merozoite
surface and within the specialized organelles of the apical complex. The Plasmodium …

The human malaria parasite Plasmodium falciparum demonstrates variability in its
dependence upon erythrocyte sialic acid residues for invasion. Some lines of P. falciparum …

Invasion of erythrocytes by malaria parasites involves multiple receptor-ligand interactions.
To elucidate these pathways, we made use of four parasite clones with differing specificities …

Invasion of the merozoite form of Plasmodium falciparum into human erythrocytes involves
multiple receptor–ligand interactions. The EBA175 protein of P. falciparum has been shown …

Plasmodium falciparum malaria parasites with different capabilities of invading sialic acid-
deficient erythrocytes were identified. Thai-2 parasites cultured in Tn erythrocytes invaded …