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Structure paper

TitleCryo-EM structure of an essential Plasmodium vivax invasion complex.
Journal, issue, pagesNature, Vol. 559, Issue 7712, Page 135-139, Year 2018
Publish dateJun 27, 2018
AuthorsJakub Gruszczyk / Rick K Huang / Li-Jin Chan / Sébastien Menant / Chuan Hong / James M Murphy / Yee-Foong Mok / Michael D W Griffin / Richard D Pearson / Wilson Wong / Alan F Cowman / Zhiheng Yu / Wai-Hong Tham /
PubMed AbstractPlasmodium vivax is the most widely distributed malaria parasite that infects humans. P. vivax invades reticulocytes exclusively, and successful entry depends on specific interactions between the P. ...Plasmodium vivax is the most widely distributed malaria parasite that infects humans. P. vivax invades reticulocytes exclusively, and successful entry depends on specific interactions between the P. vivax reticulocyte-binding protein 2b (PvRBP2b) and transferrin receptor 1 (TfR1). TfR1-deficient erythroid cells are refractory to invasion by P. vivax, and anti-PvRBP2b monoclonal antibodies inhibit reticulocyte binding and block P. vivax invasion in field isolates. Here we report a high-resolution cryo-electron microscopy structure of a ternary complex of PvRBP2b bound to human TfR1 and transferrin, at 3.7 Å resolution. Mutational analyses show that PvRBP2b residues involved in complex formation are conserved; this suggests that antigens could be designed that act across P. vivax strains. Functional analyses of TfR1 highlight how P. vivax hijacks TfR1, an essential housekeeping protein, by binding to sites that govern host specificity, without affecting its cellular function of transporting iron. Crystal and solution structures of PvRBP2b in complex with antibody fragments characterize the inhibitory epitopes. Our results establish a structural framework for understanding how P. vivax reticulocyte-binding protein engages its receptor and the molecular mechanism of inhibitory monoclonal antibodies, providing important information for the design of novel vaccine candidates.
External linksNature / PubMed:29950717
MethodsEM (single particle) / X-ray diffraction
Resolution1.87 - 3.8 Å
Structure data

7783

6d03

EMDB-7783, PDB-6d03:
Cryo-EM structure of a Plasmodium vivax invasion complex essential for entry into human reticulocytes; one molecule of parasite ligand.
Method: EM (single particle) / Resolution: 3.68 Å

7784

6d04

EMDB-7784, PDB-6d04:
Cryo-EM structure of a Plasmodium vivax invasion complex essential for entry into human reticulocytes; two molecules of parasite ligand, subclass 1.
Method: EM (single particle) / Resolution: 3.74 Å

7785

6d05

EMDB-7785, PDB-6d05:
Cryo-EM structure of a Plasmodium vivax invasion complex essential for entry into human reticulocytes; two molecules of parasite ligand, subclass 2.
Method: EM (single particle) / Resolution: 3.8 Å

PDB-6bpa:
Plasmodium vivax reticulocyte binding protein 2b (PvRBP2b) bound to monoclonal antibody 3E9
Method: X-RAY DIFFRACTION / Resolution: 2.53 Å

PDB-6bpb:
Plasmodium vivax invasion blocking monoclonal antibody 4F7
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

PDB-6bpc:
Plasmodium vivax reticulocyte binding protein 2b (PvRBP2b) bound to monoclonal antibody 4F7
Method: X-RAY DIFFRACTION / Resolution: 2.66 Å

PDB-6bpd:
Plasmodium vivax invasion blocking monoclonal antibody 10B12
Method: X-RAY DIFFRACTION / Resolution: 2.32 Å

PDB-6bpe:
Plasmodium vivax reticulocyte binding protein 2b (PvRBP2b) bound to monoclonal antibody 6H1
Method: X-RAY DIFFRACTION / Resolution: 3.34 Å

Chemicals

ChemComp-BR:
BROMIDE ION / Bromide

ChemComp-HOH:
WATER / Water

ChemComp-CA:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-FE:
Unknown entry / Iron

ChemComp-CO3:
CARBONATE ION / Carbonate

Source
  • Homo sapiens (human)
  • Human (human)
  • plasmodium vivax (malaria parasite P. vivax)
  • plasmodium vivax (strain salvador i) (eukaryote)
  • mus musculus (house mouse)
KeywordsCELL INVASION / Plasmodium vivax / invasion / malaria / antibody complex / IMMUNE SYSTEM / antibody / reticulocyte

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