5W53

Crystal structure of the erythrocyte-binding domain from Plasmodium vivax reticulocyte-binding protein 2b (PvRBP2b)

Summary for 5W53

• Entry DOI: 10.2210/pdb5w53/pdb
• Descriptor: Reticulocyte binding protein 2, putative, THIOCYANATE ION, POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: reticulocyte-binding, cell invasion, alpha-helical
• Biological source: Plasmodium vivax (strain Salvador I)
• Total number of polymer chains: 2
• Total formula weight: 73642.77

Authors

Gruszczyk, J.,Tham, W.H. (deposition date: 2017-06-13, release date: 2017-11-29, Last modification date: 2024-11-13)

Primary citation

Gruszczyk, J.,Kanjee, U.,Chan, L.J.,Menant, S.,Malleret, B.,Lim, N.T.Y.,Schmidt, C.Q.,Mok, Y.F.,Lin, K.M.,Pearson, R.D.,Rangel, G.,Smith, B.J.,Call, M.J.,Weekes, M.P.,Griffin, M.D.W.,Murphy, J.M.,Abraham, J.,Sriprawat, K.,Menezes, M.J.,Ferreira, M.U.,Russell, B.,Renia, L.,Duraisingh, M.T.,Tham, W.H.
Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax.
Science, 359:48-55, 2018

PubMed Abstract: shows a strict host tropism for reticulocytes. We identified transferrin receptor 1 (TfR1) as the receptor for reticulocyte-binding protein 2b (PvRBP2b). We determined the structure of the N-terminal domain of PvRBP2b involved in red blood cell binding, elucidating the molecular basis for TfR1 recognition. We validated TfR1 as the biological target of PvRBP2b engagement by means of TfR1 expression knockdown analysis. TfR1 mutant cells deficient in PvRBP2b binding were refractory to invasion of but not to invasion of Using Brazilian and Thai clinical isolates, we show that PvRBP2b monoclonal antibodies that inhibit reticulocyte binding also block entry into reticulocytes. These data show that TfR1-PvRBP2b invasion pathway is critical for the recognition of reticulocytes during invasion.

PubMed: 29302006
DOI: 10.1126/science.aan1078

Experimental method

X-RAY DIFFRACTION (1.71 Å)