Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein.

@article{Modis2005VariableSE,
  title={Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein.},
  author={Yorgo Modis and Steven Ogata and David Clements and Stephen C Harrison},
  journal={Journal of virology},
  year={2005},
  volume={79 2},
  pages={1223-31}
}
Dengue virus is an emerging global health threat. The major envelope glycoprotein, E, mediates viral attachment and entry by membrane fusion. Antibodies that bind but fail to neutralize noncognate serotypes enhance infection. We have determined the crystal structure of a soluble fragment of the envelope glycoprotein E from dengue virus type 3. The structure closely resembles those of E proteins from dengue type 2 and tick-borne encephalitis viruses. Serotype-specific neutralization escape… CONTINUE READING
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