Open AccessOverproduction, purification and crystallization of a chondroitin sulfate A‐binding DBL domain from a Plasmodium falciparum var2csa ‐encoded PfEMP1 protein
Author(s) -
Higgins Matthew K.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108004211
Subject(s) - plasmodium falciparum , overproduction , crystallization , domain (mathematical analysis) , chondroitin sulfate , chemistry , biochemistry , virology , biology , glycosaminoglycan , malaria , gene , immunology , organic chemistry , mathematical analysis , mathematics
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.