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6WN1

Plasmodium vivax reticulocyte binding protein 2b (PvRBP2b) bound to human monoclonal antibody 241242

Summary for 6WN1
Entry DOI10.2210/pdb6wn1/pdb
Related6WM9
DescriptorReticulocyte binding protein 2b, 241242 Fab heavy chain, 241242 Fab light chain (3 entities in total)
Functional Keywordsinvasion, plasmodium vivax, malaria, antibody complex, cell invasion
Biological sourcePlasmodium vivax Sal-1
More
Total number of polymer chains6
Total formula weight169410.58
Authors
Chan, L.J.,Dietrich, M.H.,Tham, W.H. (deposition date: 2020-04-22, release date: 2021-01-27, Last modification date: 2024-10-16)
Primary citationChan, L.J.,Gandhirajan, A.,Carias, L.L.,Dietrich, M.H.,Vadas, O.,Visentin, R.,Franca, C.T.,Menant, S.,Soldati-Favre, D.,Mueller, I.,King, C.L.,Tham, W.H.
Naturally acquired blocking human monoclonal antibodies to Plasmodium vivax reticulocyte binding protein 2b.
Nat Commun, 12:1538-1538, 2021
Cited by
PubMed Abstract: Plasmodium vivax preferentially invades reticulocytes and recognition of these cells is mediated by P. vivax Reticulocyte Binding Protein 2b (PvRBP2b) binding to human Transferrin receptor 1 (TfR1) and Transferrin (Tf). Longitudinal cohort studies in Papua New Guinea, Thailand and Brazil show that PvRBP2b antibodies are correlated with protection against P. vivax infection and disease. Here, we isolate and characterize anti-PvRBP2b human monoclonal antibodies from two individuals in Cambodia with natural P. vivax infection. These antibodies bind with high affinities and map to different regions of PvRBP2b. Several human antibodies block PvRBP2b binding to reticulocytes and inhibit complex formation with human TfR1-Tf. We describe different structural mechanisms for functional inhibition, including either steric hindrance with TfR1-Tf or the reticulocyte membrane. These results show that naturally acquired human antibodies against PvRBP2b can inhibit its function which is important for P. vivax invasion.
PubMed: 33750786
DOI: 10.1038/s41467-021-21811-2
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.15 Å)
Structure validation

226707

건을2024-10-30부터공개중

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