Plasmodium falciparum virulence is associated with sequestration of infected erythrocytes. Microvascular binding mediated by PfEMP1 in complex with non-immune immunoglobulin M (IgM) is common among ...Plasmodium falciparum virulence is associated with sequestration of infected erythrocytes. Microvascular binding mediated by PfEMP1 in complex with non-immune immunoglobulin M (IgM) is common among parasites that cause both severe childhood malaria and pregnancy-associated malaria. Here, we present cryo-molecular electron tomography structures of human IgM, PfEMP1 and their complex. Three-dimensional reconstructions of IgM reveal that it has a dome-like core, randomly oriented Fab2s units, and the overall shape of a turtle. PfEMP1 is a C- shaped molecule with a flexible N terminus followed by an arc-shaped backbone and a bulky C terminus that interacts with IgM. Our data demonstrate that the PfEMP1 binding pockets on IgM overlap with those of C1q, and the bulkiness of PfEMP1 limits the capacity of IgM to interact with PfEMP1. We suggest that P. falciparum exploits IgM to cluster PfEMP1 into an organized matrix to augment its affinity to host cell receptors.
EMDB-2882: Cryo-Molecular electron tomography of NTS-DBL1alphaCIDRgamma (N-terminal domain of PfEMP1-IT4Var60) Method: EM (tomography) / Resolution: 20.0 Å
EMDB-2883: Cryo-Molecular electron tomography of NTS-DBL1alphaCIDRgamma (N-terminal domain of PfEMP1-IT4Var60) Method: EM (tomography) / Resolution: 20.0 Å
EMDB-2884: Cryo-Molecular electron tomography of PfEMP1-IT4Var60) Method: EM (tomography) / Resolution: 20.0 Å
EMDB-2885: Cryo-Molecular electron tomography of PfEMP1-IT4Var60) Method: EM (tomography) / Resolution: 20.0 Å
EMDB-2886: Cryo-Molecular electron tomography of PfEMP1-IT4Var60) Method: EM (subtomogram averaging) / Resolution: 20.0 Å
EMDB-2887: Cryo-Molecular electron tomography of human non-immune soluble pentameric IgM Method: EM (tomography) / Resolution: 25.0 Å
EMDB-2888: Cryo-Molecular electron tomography of human non-immune soluble pentameric IgM Method: EM (tomography) / Resolution: 20.0 Å
EMDB-2889: Cryo-Molecular electron tomography of human non-immune soluble pentameric IgM Method: EM (tomography) / Resolution: 20.0 Å
EMDB-2890: Cryo-Molecular electron tomography of human non-immune soluble pentameric IgM Method: EM (tomography) / Resolution: 20.0 Å
EMDB-2891: Cryo-Molecular electron tomography of complex of human non-immune soluble pentameric IgM and PfEMP1-IT4Var60 in 1:1 ratio Method: EM (tomography) / Resolution: 20.0 Å
EMDB-2892: Cryo-Molecular electron tomography of complex of human non-immune soluble pentameric IgM and PfEMP1-IT4Var60 in 1:1 ratio Method: EM (tomography) / Resolution: 20.0 Å
EMDB-2893: Cryo-Molecular electron tomography of complex of human non-immune soluble pentameric IgM and PfEMP1-IT4Var60 in 1:1 ratio Method: EM (tomography) / Resolution: 25.0 Å
EMDB-2894: Cryo-Molecular electron tomography of complex of human non-immune soluble pentameric IgM and PfEMP1-IT4Var60 in 1:2 ratio Method: EM (tomography) / Resolution: 25.0 Å
EMDB-2895: Cryo-Molecular electron tomography of complex of human non-immune soluble pentameric IgM and PfEMP1-IT4Var60 in 1:2 ratio Method: EM (tomography) / Resolution: 20.0 Å
EMDB-6554: Cryo-Molecular electron tomography of IgM Method: EM (tomography) / Resolution: 25.0 Å
Source
Plasmodium falciparum (malaria parasite P. falciparum)
Homo sapiens (human)
+
About Yorodumi Papers
-
News
-
Feb 9, 2022. New format data for meta-information of EMDB entries
New format data for meta-information of EMDB entries
Version 3 of the EMDB header file is now the official format.
The previous official version 1.9 will be removed from the archive.
In the structure databanks used in Yorodumi, some data are registered as the other names, "COVID-19 virus" and "2019-nCoV". Here are the details of the virus and the list of structure data.
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)
EMDB accession codes are about to change! (news from PDBe EMDB page)
The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
The EM Navigator/Yorodumi systems omit the EMD- prefix.
Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator