High resolution crystal structure of dengue-3 envelope protein domain III suggests possible molecular mechanisms for serospecific antibody recognition

Dengue viruses are classified into four serotypes. Here, we report a 1.7 Å crystal structure of a recombinant dengue‐3 envelope protein domain III (ED3), which contains most of the putative epitopes. Although the fold was well conserved, we found that a local backbone deformation in the first β‐strand, which contains the putative epitope‐1, occurred upon domain isolation. Furthermore, a comparison with dengue‐2 ED3 indicated a large structural change by as much as 4.0 Å at Asp662, located in epitope‐2. These minute structural and surface properties changes observed in the high resolution ED3 structure represent potential determinants for serospecificity and epitope recognition by antibodies. © 2012 Wiley Periodicals, Inc.