Antigenic drift in the ligand domain of Plasmodium vivax duffy binding protein confers resistance to inhibitory antibodies.

@article{Vanbuskirk2004AntigenicDI,
  title={Antigenic drift in the ligand domain of Plasmodium vivax duffy binding protein confers resistance to inhibitory antibodies.},
  author={Kelley Vanbuskirk and Jennifer L Cole-Tobian and Moses Baisor and Elitza S Sevova and Moses John Bockarie and Christopher L King and John H Adams},
  journal={The Journal of infectious diseases},
  year={2004},
  volume={190 9},
  pages={1556-62}
}
Interaction of the Duffy binding protein (DBP) with its erythrocyte receptor is critical for maintaining Plasmodium vivax blood-stage infections, making DBP an appealing vaccine candidate. The cysteine-rich region II is the ligand domain of DBP and a target of vaccine development. Interestingly, most of the allelic diversity observed in DBP is due to the high rate of nonsynonymous polymorphisms in this critical domain for receptor recognition. Similar to the hypervariability in influenza… CONTINUE READING

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