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  Structure of the merozoite surface protein 1 from Plasmodium falciparum

Dijkman, P. M., Marzluf, T., Zhang, Y., Chang, S.-Y.-S., Helm, D., Lanzer, M., et al. (2021). Structure of the merozoite surface protein 1 from Plasmodium falciparum. Science Advances, 7(23): eabg0465. doi:10.1126/sciadv.abg0465.

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 Creators:
Dijkman, Pratricia M.1, 2, Author           
Marzluf, Tanja3, 4, Author
Zhang, Yingyi1, 2, Author           
Chang, Shih-Ying Scott1, 2, Author           
Helm, Dominic4, Author
Lanzer, Michael3, Author
Bujard, Hermann5, 6, Author
Kudryashev, Mikhail1, 2, Author           
Affiliations:
1Sofja Kovalevskaja Group, Max Planck Institute of Biophysics, Max Planck Society, ou_2253651              
2Buchmann Institute for Molecular Life Sciences (BMLS), Goethe University of Frankfurt, Frankfurt am Main, Germany, ou_persistent22              
3Centre for Infectious Diseases, Parasitology Unit, Heidelberg University Hospital, Heidelberg University, Heidelberg, Germany, ou_persistent22              
4MS-based Protein Analysis Unit, Genomics and Proteomics Core Facility, German Cancer Research Center (DKFZ), Heidelberg, Germany, ou_persistent22              
5Sumaya Biotech GmbH & Co. KG, Heidelberg, Germany, ou_persistent22              
6Centre for Molecular Biology Heidelberg, Heidelberg University, Heidelberg, Germany, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2020-12-082021-04-142021-06-02
 Publication Status: Published online
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1126/sciadv.abg0465
 Degree: -

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Title: Science Advances
  Other : Sci. Adv.
Source Genre: Journal
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Publ. Info: Washington : AAAS
Pages: - Volume / Issue: 7 (23) Sequence Number: eabg0465 Start / End Page: - Identifier: ISSN: 2375-2548
CoNE: https://pure.mpg.de/cone/journals/resource/2375-2548