Helmholtz Gemeinschaft


Structure of the merozoite surface protein 1 from Plasmodium falciparum

PDF (Original Article) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
[img] Other (Supplementary Materials)

Item Type:Article
Title:Structure of the merozoite surface protein 1 from Plasmodium falciparum
Creators Name:Dijkman, P.M. and Marzluf, T. and Zhang, Y. and Chang, S.Y.S. and Helm, D. and Lanzer, M. and Bujard, H. and Kudryashev, M.
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.
Keywords:Amino Acid Sequence, Erythrocytes, Malaria, Merozoite Surface Protein 1, Plasmodium falciparum, Protozoan Proteins
Source:Science Advances
Publisher:American Association for the Advancement of Science
Page Range:eabg0465
Date:June 2021
Official Publication:https://doi.org/10.1126/sciadv.abg0465
PubMed:View item in PubMed

Repository Staff Only: item control page


Downloads per month over past year

Open Access
MDC Library