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={S. Lok and V. Kostyuchenko and G. Nybakken and H. Holdaway and A. Battisti and Soila Sukupolvi-Petty and D. Sedlak and D. Fremont and P. Chipman and J. Roehrig and M. Diamond and R. Kuhn and M. Rossmann},
  journal={Nature Structural &Molecular Biology},
  year={2008},
  volume={15},
  pages={312-317}
}
  • S. Lok, V. Kostyuchenko, +10 authors M. Rossmann
  • Published 2008
  • Medicine, Biology
  • Nature Structural &Molecular Biology
  • 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… CONTINUE READING
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