A heparin-binding protein of Plasmodium berghei is associated with merozoite invasion of erythrocytes

Background Malaria caused by Plasmodium species is a prominent public health concern worldwide, and the infection of a malarial parasite is transmitted to humans through the saliva of female Anopheles mosquitoes. Plasmodium invasion is a rapid and complex process. A critical step in the blood-stage infection of malarial parasites is the adhesion of merozoites to red blood cells (RBCs), which involves interactions between parasite ligands and receptors. The present study aimed to investigate a previously uncharacterized protein, Pb MAP1 (encoded by PBANKA_1425900), which facilitates Plasmodium berghei ANKA ( Pb ANKA) merozoite attachment and invasion via the heparan sulfate receptor. Methods Pb MAP1 protein expression was investigated at the asexual blood stage, and its specific binding activity to both heparan sulfate and RBCs was analyzed using western blotting, immunofluorescence, and flow cytometry. Furthermore, a Pb MAP1-knockout parasitic strain was established using the double-crossover method to investigate its pathogenicity in mice. Results The Pb MAP1 protein, primarily localized to the P. berghei membrane at the merozoite stage, is involved in binding to heparan sulfate-like receptor on RBC surface of during merozoite invasion. Furthermore, mice immunized with the Pb MAP1 protein or passively immunized with sera from Pb MAP1-immunized mice exhibited increased immunity against lethal challenge. The Pb MAP1-knockout parasite exhibited reduced pathogenicity. Conclusions Pb MAP1 is involved in the binding of P. berghei to heparan sulfate-like receptors on RBC surface during merozoite invasion.