Author/Authors :
Richard J. Kuhn and Michael G. Rossmann، نويسنده , , Wei Zhang، نويسنده , , Michael G. Rossmann، نويسنده , , Sergei V. Pletnev، نويسنده , , Jeroen Corver، نويسنده , , Edith Lenches، نويسنده , , Christopher T. Jones، نويسنده , , Suchetana Mukhopadhyay، نويسنده , , Paul R. Chipman، نويسنده , , Ellen G. Strauss، نويسنده , , Max L. Nibert and Timothy S. Baker، نويسنده , , James H. Strauss، نويسنده ,
Abstract :
The first structure of a flavivirus has been determined by using a combination of cryoelectron microscopy and fitting of the known structure of glycoprotein E into the electron density map. The virus core, within a lipid bilayer, has a less-ordered structure than the external, icosahedral scaffold of 90 glycoprotein E dimers. The three E monomers per icosahedral asymmetric unit do not have quasiequivalent symmetric environments. Difference maps indicate the location of the small membrane protein M relative to the overlaying scaffold of E dimers. The structure suggests that flaviviruses, and by analogy also alphaviruses, employ a fusion mechanism in which the distal β barrels of domain II of the glycoprotein E are inserted into the cellular membrane.
