Binding of subdomains 1/2 of PfEMP1-DBL1α to heparan sulfate or heparin mediates Plasmodium falciparum rosetting.

ABSTRACT: The capacity of Plasmodium falciparum parasitized erythrocytes (pRBC) to adhere to the endothelial lining in the microvasculature and to red blood cells (RBC) is associated with the virulence of the parasite, the pathogenesis and development of severe malaria. Rosetting, the binding of uninfected RBC to pRBC, is frequently observed in individuals with severe malaria and is mediated by the N-terminal NTS-DBL1α domain of the adhesin Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) expressed at the surface of the pRBC. Heparan sulfate has been suggested to be an important receptor for the NTS-DBL1α variant IT4(var60) expressed by the parasite FCR3S1.2. Here, we have determined the binding site of NTS-DBL1α (IT4(var60)) to the RBC and heparin using a set of recombinant, mutated pr

SUBMITTER: Angeletti D 

PROVIDER: S-EPMC4351205 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature