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