Cloning the P. falciparum gene encoding PfEMP1, a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes

DI Baruch, BL Pasloske, HB Singh, X Bi, XC Ma… - Cell, 1995 - cell.com
DI Baruch, BL Pasloske, HB Singh, X Bi, XC Ma, M Feldman, TF Taraschi, RJ Howard
Cell, 1995cell.com
Plasmodium falciparum-infected human erythrocytes evade host immunity by expression of
a ceil-surface variant antigen and receptors for adherence to endothelial cells. These
properties have been ascribed to P. fakiparum erythrocyte membrane protein 1 (PfEMPl), an
antigenically diverse malarial protein of 200450 kDa on the surface of parasitized
erythrocytes (PEs). We describe the cloning of two related PfEMPl genes from the Yalayan
Camp (MC) parasite strain. Antibodies generated against recombinant protein fragments of …
Summary
Plasmodium falciparum-infected human erythrocytes evade host immunity by expression of a ceil-surface variant antigen and receptors for adherence to endothelial cells. These properties have been ascribed to P. fakiparum erythrocyte membrane protein 1 (PfEMPl), an antigenically diverse malarial protein of 200450 kDa on the surface of parasitized erythrocytes (PEs). We describe the cloning of two related PfEMPl genes from the Yalayan Camp (MC) parasite strain. Antibodies generated against recombinant protein fragments of the genes were specific for MC strain PfEMPl protein. These antibodies reacted only with the surface of MC strain PEs and blocked adherence of these cells to CD36 but without effect on adherence to thrombospondin. Multiple forms of the PfEMPl gene are apparent in MC parasites. The molecular basis for antigenic variation in malaria and adherence of infected erythrocytes to host cells can now be pursued.
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