Identifying merozoite surface protein 4 and merozoite surface protein 7 Plasmodium falciparum protein family members specifically binding to human erythrocytes suggests a new malarial parasite-redundant survival mechanism.

Plasmodium falciparum merozoite surface proteins (MSP-1 to -11) have been involved in merozoite interaction with the red blood cell (RBC) surface. Peptides covering complete MSP-4 and MSP-7 amino acid sequences were synthesized and tested in RBC binding assays. One MSP-4 high activity binding peptide (HABP) and five MSP-7 HABPs were found having specific binding to RBC surface. MSP-4 and MSP-7 HABP binding was sensitive to enzymatic treatment; they recognized a 52 kDa erythrocyte membrane protein. MSP-4 HABP had low invasion inhibition, suggesting it might bind to RBCs and also be involved in physiological mechanisms, while MSP-7 HABPs displayed different invasion inhibition activity (83-24%) in in vitro tests, suggesting different roles for both proteins during invasion. Structural characteristics found when comparing the MSP-4 HABP with MSP-HABPs displaying epidermal growth factor-like sequences suggested that these redundant MSP-family proteins could be a new parasite strategy for evading host genetic variability and immune pressure.

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