Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins

@article{Lok2008BindingOA,
  title={Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins},
  author={Shee-Mei Lok and V. K. Kostyuchenko and Grant E. Nybakken and Heather A. Holdaway and Anthony J. Battisti and Soila Sukupolvi-Petty and Dagmar Sedlak and Daved H. Fremont and Paul Chipman and John T. Roehrig and Michael Steven Diamond and Richard J. Kuhn and Michael G. Rossmann},
  journal={Nature Structural \&Molecular Biology},
  year={2008},
  volume={15},
  pages={312-317}
}
The monoclonal antibody 1A1D-2 has been shown to strongly neutralize dengue virus serotypes 1, 2 and 3, primarily by inhibiting attachment to host cells. A crystal structure of its antigen binding fragment (Fab) complexed with domain III of the viral envelope glycoprotein, E, showed that the epitope would be partially occluded in the known structure of the mature dengue virus. Nevertheless, antibody could bind to the virus at 37 °C, suggesting that the virus is in dynamic motion making hidden… 
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