Full-length extracellular region of the var2CSA variant of PfEMP1 is required for specific, high-affinity binding to CSA.

@article{Srivastava2010FulllengthER,
  title={Full-length extracellular region of the var2CSA variant of PfEMP1 is required for specific, high-affinity binding to CSA.},
  author={Anand Srivastava and St{\'e}phane Gangnard and Adam Round and S{\'e}bastien Dechavanne and Alexandre Juillerat and Bertrand Raynal and Grazyna Faure and Bruno Baron and St{\'e}phanie Ramboarina and Saurabh Singh and Hassan Belrhali and Patrick England and Anita Lewit-Bentley and Artur Scherf and Graham A Bentley and Beno{\^i}t Gamain},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 11},
  pages={4884-9}
}
Pregnancy-associated malaria (PAM) is a serious consequence of sequestration of Plasmodium falciparum-parasitized erythrocytes (PE) in the placenta through adhesion to chondroitin sulfate A (CSA) present on placental proteoglycans. Recent work implicates var2CSA, a member of the PfEMP1 family, as the mediator of placental sequestration and as a key target for PAM vaccine development. Var2CSA is a 350 kDa transmembrane protein, whose extracellular region includes six Duffy-binding-like (DBL… CONTINUE READING
60 Citations
40 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 60 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 40 references

Structure of the DBL3x domain of pregnancy-associated malaria protein VAR2CSA complexed with chondroitin sulfate A

  • K Singh
  • Nat Struct Mol Biol
  • 2008

The structure of a chondroitin sulfate-binding domain important in placental malaria

  • MK Higgins
  • J Biol Chem
  • 2008

Similar Papers

Loading similar papers…