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• W2148019354 abstract "The human malaria parasite Plasmodium falciparum can cause infected red blood cells (iRBC) to form rosettes with uninfected RBC, a phenotype associated with severe malaria. Rosetting is mediated by a subset of the Plasmodium falciparum membrane protein 1 (PfEMP1) variant adhesins expressed on the infected host-cell surface. Heparin and other sulfated oligosaccharides, however, can disrupt rosettes, suggesting that therapeutic approaches to this form of severe malaria are feasible. We present a structural and functional study of the N-terminal domain of PfEMP1 from the VarO variant comprising the N-terminal segment (NTS) and the first DBL domain (DBL1 α 1 ), which is directly implicated in rosetting. We demonstrate that NTS-DBL1 α 1 -VarO binds to RBC and that heparin inhibits this interaction in a dose-dependent manner, thus mimicking heparin-mediated rosette disruption. We have determined the crystal structure of NTS-DBL1 α 1 , showing that NTS, previously thought to be a structurally independent component of PfEMP1, forms an integral part of the DBL1α domain. Using mutagenesis and docking studies, we have located the heparin-binding site, which includes NTS. NTS, unique to the DBL α-class domain, is thus an intrinsic structural and functional component of the N-terminal VarO domain. The specific interaction observed with heparin opens the way for developing antirosetting therapeutic strategies." @default.
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• W2148019354 date "2011-03-14" @default.
• W2148019354 modified "2023-10-18" @default.
• W2148019354 title "Structure of a <i>Plasmodium falciparum</i> PfEMP1 rosetting domain reveals a role for the N-terminal segment in heparin-mediated rosette inhibition" @default.
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• W2148019354 doi "https://doi.org/10.1073/pnas.1018692108" @default.
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