Conformational changes of the flavivirus E glycoprotein

Structure. 2004 Sep;12(9):1607-18. doi: 10.1016/j.str.2004.06.019.

Abstract

Dengue virus, a member of the Flaviviridae family, has a surface composed of 180 copies each of the envelope (E) glycoprotein and the membrane (M) protein. The crystal structure of an N-terminal fragment of E has been determined and compared with a previously described structure. The primary difference between these structures is a 10 degrees rotation about a hinge relating the fusion domain DII to domains DI and DIII. These two rigid body components were used for independent fitting of E into the cryo-electron microscopy maps of both immature and mature dengue viruses. The fitted E structures in these two particles showed a difference of 27 degrees between the two components. Comparison of the E structure in its postfusion state with that in the immature and mature virions shows a rotation approximately around the same hinge. Flexibility of E is apparently a functional requirement for assembly and infection of flaviviruses.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Dengue Virus / chemistry*
  • Dengue Virus / metabolism
  • Dengue Virus / ultrastructure
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation*
  • Sequence Alignment
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / metabolism
  • Virion / chemistry

Substances

  • E-glycoprotein, Dengue virus type 2
  • Viral Envelope Proteins

Associated data

  • PDB/1TG8
  • PDB/1TGE
  • PDB/1THD