Recombinant hepatitis E capsid protein self-assembles into a dual-domain T = 1 particle presenting native virus epitopes.
The three-dimensional structure of a self-assembled, recombinant hepatitis E virus particle has been solved to 22-A resolution by cryo-electron microscopy and three-dimensional image reconstruction. The single subunit of 50 kDa is derived from a truncated version of the open reading frame-2 gene of the virus expressed in a baculovirus system. This is the first structure of a T = 1 particle with protruding dimers at the icosahedral two-fold axes solved by cryo-electron microscopy. The protein shell of these hollow particles extends from a radius of 50 A outward to a radius of 135 A. In the reconstruction, the capsid is dominated by dimers that define the 30 morphological units. The outer domain of the homodimer forms a protrusion, which corresponds to the spike-like density seen in the cryo-electron micrograph. This particle retains native virus epitopes, suggesting its potential value as a vaccine.
Xing
L
L
Department of Biosciences at Novum, Karolinska Institute, Huddinge, 14157, Sweden.
Kato
K
K
Li
T
T
Takeda
N
N
Miyamura
T
T
Hammar
L
L
Cheng
R H
RH
D002213:Capsid / Q000648:ultrastructure*; D020285:Cryoelectron Microscopy; D000939:Epitopes / Q000648:ultrastructure; D016752:Hepatitis E virus / Q000648:ultrastructure*; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D008970:Molecular Weight; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000648:ultrastructure; D014771:Virion / Q000648:ultrastructure
D000939:Epitopes; D011994:Recombinant Proteins