Conformational Changes of the Flavivirus E Glycoprotein

• Published in: Structure (London) 2004-09, Vol.12 (9), p.1607-1618
• Main Authors: Zhang, Ying, Zhang, Wei, Ogata, Steven, Clements, David, Strauss, James H., Baker, Timothy S., Kuhn, Richard J., Rossmann, Michael G.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Cryoelectron Microscopy; Crystallography, X-Ray; Dengue virus; Dengue Virus - chemistry; Dengue Virus - metabolism; Dengue Virus - ultrastructure; Flavivirus; Humans; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Alignment; Viral Envelope Proteins - chemistry; Viral Envelope Proteins - metabolism; Virion - chemistry
• ISSN: 0969-2126; 1878-4186
• DOI: 10.1016/j.str.2004.06.019

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° 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° 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.