Conformational changes of the flavivirus E glycoprotein.
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.
Zhang
Ying
Y
Department of Biological Sciences, Lilly Hall, 915 West State Street, Purdue University, West Lafayette, IN 47907, USA.
Zhang
Wei
W
Ogata
Steven
S
Clements
David
D
Strauss
James H
JH
Baker
Timothy S
TS
Kuhn
Richard J
RJ
Rossmann
Michael G
MG
D000595:Amino Acid Sequence; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D003716:Dengue Virus / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000378:metabolism; D014771:Virion / Q000737:chemistry
C051821:E-glycoprotein, Dengue virus type 2; D014759:Viral Envelope Proteins