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

doi:10.1126/sciadv.abg0465

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^*

^*Corresponding author for this work

Research output: Contribution to journal › Journal Article › peer-review

26 Citations (Scopus)

Abstract

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.

Original language	English
Article number	eabg0465
Journal	Science Advances
Volume	7
Issue number	23
DOIs	https://doi.org/10.1126/sciadv.abg0465
Publication status	Published - Jun 2021
Externally published	Yes

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Publisher Copyright:
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).

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title = "Structure of the merozoite surface protein 1 from Plasmodium falciparum",

abstract = "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.",

author = "Dijkman, \{Patricia M.\} and Tanja Marzluf and Yingyi Zhang and Chang, \{Shih Ying Scott\} and Dominic Helm and Michael Lanzer and Hermann Bujard and Mikhail Kudryashev",

note = "Publisher Copyright: Copyright {\textcopyright} 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).",

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doi = "10.1126/sciadv.abg0465",

language = "English",

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AU - Dijkman, Patricia M.

AU - Marzluf, Tanja

AU - Zhang, Yingyi

AU - Chang, Shih Ying Scott

AU - Helm, Dominic

AU - Lanzer, Michael

AU - Bujard, Hermann

AU - Kudryashev, Mikhail

N1 - Publisher Copyright: 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).

PY - 2021/6

Y1 - 2021/6

N2 - 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.

AB - 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.

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UR - https://openalex.org/W3164812140

UR - https://www.scopus.com/pages/publications/85107293685

U2 - 10.1126/sciadv.abg0465

DO - 10.1126/sciadv.abg0465

M3 - Journal Article

SN - 2375-2548

VL - 7

JO - Science Advances

JF - Science Advances

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M1 - eabg0465

ER -

Structure of the merozoite surface protein 1 from Plasmodium falciparum

Abstract

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