Merozoite surface protein 2 (MSP2) is a potential vaccine candidate against malaria, although its functional role is yet to be elucidated. Previous studies showed that MSP2 can interact with membranes, which may facilitate merozoite invasion into the host cell. The N-terminal 25 residues of MSP2 (MSP21-25 ), which may be aggregated on the merozoite surface, play a key role in the interaction with membranes. Here, we investigated the effects of MSP21-25 -membrane interactions on the conformation and aggregation of MSP21-25 and on membrane integrity, using nanodiscs and small unilamellar vesicles as mimetics of cell membranes. MSP21-25 -membrane interactions induced the peptide to form β-structure and to aggregate, depending on the lipid composition of the membrane. Nonfibrillar aggregates in turn disrupted the membrane.
Keywords: aggregation; amyloid fibril; membrane disruption; membrane interaction; merozoite surface protein 2.
© 2018 Federation of European Biochemical Societies.