A recombinant Duffy binding–like (DBL)–γ domain from a previously identified placental
isolate, 732, was expressed by use of the baculovirus/insect cell system and was purified in …

We used a panel of nine fusion proteins that contain different Duffy binding-like α (DBL-α)
domains of Plasmodium falciparum-infected erythrocyte membrane protein 1 to assess the …

Maternal malaria is associated with the sequestration, in the placenta, of Plasmodium
falciparum-infected erythrocytes onto chondroitin sulfate A (CSA), via the duffy binding-like …

Plasmodium falciparum parasites remodel the surface of human erythrocytes on invasion by
the insertion of parasite-derived proteins in knob-like protrusions. P. falciparum erythrocyte …

Individuals living in areas with high Plasmodium falciparum transmission acquire immunity
to malaria over time and adults have a markedly reduced risk of contracting severe disease …

Plasmodium falciparum–infected erythrocytes adhere to syncytiotrophoblast cells lining the
placenta via glycosaminoglycans, such as chondroitin sulfate A (CSA) and hyaluronic acid …

The Duffy binding-like (DBL) domains are common adhesion modules present in
Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) variants, which are …

Open reading frames in the Plasmodium falciparum genome encode domains homologous
to the adhesive domains of the P. falciparum EBA-175 erythrocyte-binding protein (eba-175 …

Malaria merozoites require the presence of specific surface receptors on the red blood cell
for invasion. Plasmodium vivax, requires the Duffy blood group antigen as an obligate …

Plasmodium vivax invasion of human erythrocytes requires interaction of the P. vivax Duffy
binding protein (PvDBP) with its host receptor, the Duffy antigen (Fy) on the erythrocyte …