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Phenotypic variation of Plasmodium falciparum merozoite proteins directs receptor targeting for invasion of human erythrocytes
Author(s) -
Duraisingh Manoj T.,
Triglia Tony,
Ralph Stuart A.,
Rayner Julian C.,
Barnwell John W.,
McFadden Geoffrey I.,
Cowman Alan F.
Publication year - 2003
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdg096
Subject(s) - biology , plasmodium falciparum , apicomplexa , phenotype , receptor , reticulocyte , gene , antigenic variation , virulence , genetics , microbiology and biotechnology , malaria , immunology , messenger rna
The members of the phylum Apicomplexa parasitize a wide range of eukaryotic host cells. Plasmodium falciparum , responsible for the most virulent form of malaria, invades human erythrocytes using several specific and high affinity ligand–receptor interactions that define invasion pathways. We find that members of the P.falciparum reticulocyte‐binding homolog protein family, PfRh2a and PfRh2b, are expressed variantly in different lines. Targeted gene disruption shows that PfRh2b mediates a novel invasion pathway and that it functions independently of other related proteins. Phenotypic variation of the PfRh protein family allows P.falciparum to exploit different patterns of receptors on the erythrocyte surface and thereby respond to polymorphisms in erythrocyte receptors and to evade the host immune system.