| Literature DB >> 29302006 |
Jakub Gruszczyk1, Usheer Kanjee2, Li-Jin Chan1,3, Sébastien Menant1, Benoit Malleret4,5, Nicholas T Y Lim1, Christoph Q Schmidt6, Yee-Foong Mok7, Kai-Min Lin8, Richard D Pearson9,10, Gabriel Rangel2, Brian J Smith11, Melissa J Call1,3, Michael P Weekes8, Michael D W Griffin7, James M Murphy1,3, Jonathan Abraham12, Kanlaya Sriprawat13, Maria J Menezes14, Marcelo U Ferreira14, Bruce Russell15, Laurent Renia5, Manoj T Duraisingh2, Wai-Hong Tham1,3.
Abstract
Plasmodium vivax shows a strict host tropism for reticulocytes. We identified transferrin receptor 1 (TfR1) as the receptor for P. vivax 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 P. vivax but not to invasion of P. falciparum Using Brazilian and Thai clinical isolates, we show that PvRBP2b monoclonal antibodies that inhibit reticulocyte binding also block P. vivax entry into reticulocytes. These data show that TfR1-PvRBP2b invasion pathway is critical for the recognition of reticulocytes during P. vivax invasion.Entities:
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Year: 2018 PMID： 29302006 PMCID： PMC5788258 DOI： 10.1126/science.aan1078
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728