Benoît Malleret, Abbas El Sahili, Matthew Zirui Tay, Guillaume Carissimo, Alice Soh Meoy Ong, Wisna Novera, Jianqing Lin, Rossarin Suwanarusk, Varakorn Kosaisavee, Trang T T Chu, Ameya Sinha, Shanshan Wu Howland, Yiping Fan, Jakub Gruszczyk, Wai-Hong Tham, Yves Colin, Sebastian Maurer-Stroh, Georges Snounou, Lisa F P Ng, Jerry Kok Yen Chan, Ann-Marie Chacko, Julien Lescar, Rajesh Chandramohanadas, François Nosten, Bruce Russell, Laurent Rénia
More than one-third of the world's population is exposed to Plasmodium vivax malaria, mainly in Asia1 . P. vivax preferentially invades reticulocytes (immature red blood cells)2-4 . Previous work has identified 11 parasite proteins involved in reticulocyte invasion, including erythrocyte binding protein 2 (ref. 5 ) and the reticulocyte-binding proteins (PvRBPs)6-10 . PvRBP2b binds to the transferrin receptor CD71 (ref. 11 ), which is selectively expressed on immature reticulocytes12 . Here, we identified CD98 heavy chain (CD98), a heteromeric amino acid transporter from the SLC3 family (also known as SLCA2), as a reticulocyte-specific receptor for the PvRBP2a parasite ligand using mass spectrometry, flow cytometry, biochemical and parasite invasion assays...
August 2021: Nature Microbiology