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The Plasmodium berghei merozoite protein PbMAP2 associates host erythrocyte binding and invasion

ABSTRACT: The invasion of Plasmodium merozoites into host erythrocytes is initiated through specific ligand–receptor interactions. This interaction results in subsequent invasion events, facilitated by forming a moving junction through AMA–1 and associated molecular complexes mediating parasite entry into the erythrocytic membrane. Previous studies have implicated erythrocyte surface glycosaminoglycans, particularly heparan sulfate proteoglycans, as critical receptor components in this invasion process. In this study, we sought to elucidate the molecular function of PbMAP2 (encoded by PbANKA_1137800), a previously uncharacterized Plasmodium berghei ANKA protein, in mediating merozoite attachment and invasion via heparan sulfate–dependent pathways. The PbMAP2 protein, predominantly situated at the extreme apical region of the P. berghei merozoite, binds to heparin and the erythrocyte surface during merozoite invasion. Additionally, mice either immunized with the PbMAP2 protein or passively immunized with sera derived from vaccinated mice demonstrated enhanced immunity against lethal challenges. Global mass spectrometric analysis indicates that PbMAP2 engages with several trafficking and secretion proteins associated with parasite invasion. Our findings pinpointed PbMAP2 is predominantly expressed at the extreme apical region of the P. berghei merozoite and engages in binding to the heparin–like receptors on the erythrocyte surface during merozoite invasion.

ORGANISM(S): Plasmodium Sp. Kys10

SUBMITTER: Qijun Chen

PROVIDER: PXD061524 | iProX | Thu Mar 06 00:00:00 GMT 2025

REPOSITORIES: iProX

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