Structure of the merozoite surface protein 1 from Plasmodium falciparum.

Patricia M Dijkman, Tanja Marzluf, Yingyi Zhang, Shih-Ying Scott Chang, Dominic Helm, Michael Lanzer, Hermann Bujard, Mikhail Kudryashev

Science advances 2021 Jun

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The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading Plasmodium merozoite, the causative agent of malaria. MSP-1 is essential for merozoite formation, entry into and escape from erythrocytes, and is a promising vaccine candidate. Here, we present monomeric and dimeric structures of full-length MSP-1. MSP-1 adopts an unusual fold with a large central cavity. Its fold includes several coiled-coils and shows structural homology to proteins associated with membrane and cytoskeleton interactions. MSP-1 formed dimers through these domains in a concentration-dependent manner. Dimerization is affected by the presence of the erythrocyte cytoskeleton protein spectrin, which may compete for the dimerization interface. Our work provides structural insights into the possible mode of interaction of MSP-1 with erythrocytes and establishes a framework for future investigations into the role of MSP-1 in Plasmodium infection and immunity. Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

Citation

Patricia M Dijkman, Tanja Marzluf, Yingyi Zhang, Shih-Ying Scott Chang, Dominic Helm, Michael Lanzer, Hermann Bujard, Mikhail Kudryashev. Structure of the merozoite surface protein 1 from Plasmodium falciparum. Science advances. 2021 Jun;7(23)