Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 3 (March 2008)


crystallization communications



Acta Cryst. (2008). F64, 221-223    [ doi:10.1107/S1744309108004211 ]

Overproduction, purification and crystallization of a chondroitin sulfate A-binding DBL domain from a Plasmodium falciparum var2csa-encoded PfEMP1 protein

M. K. Higgins

Abstract: The PfEMP1 proteins of the malaria parasite Plasmodium falciparum are inserted into the membrane of infected red blood cells, where they mediate adhesion to a variety of human receptors. The DBL domains of the var2csa-encoded PfEMP1 protein play a critical role in malaria of pregnancy, tethering infected cells to the surface of the placenta through interactions with the glycosaminoglycan carbohydrate chondroitin sulfate A (CSA). A CSA-binding DBL domain has been overproduced in a bacterial expression system, purified and crystallized. Native data sets extending to 1.9 Å resolution have been collected and phasing is under way.

Keywords: Plasmodium falciparum; PfEMP1 protein; chondroitin sulfate A.

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