The three-dimensional structure of Infectious flacherie virus capsid determined by cryo-electron microscopy.
Cryo-electron microscopy and image reconstruction were used to determine the three-dimensional structure of Infectious flacherie virus (IFV). 5047 particles were selected for the final reconstruction. The FSC curve showed that the resolution of this capsid structure was 18 A. The structure is a psuedo T=3 (P=3) icosahedral capsid with a diameter of 302.4 A and a single shell thickness of 15 A. The density map showed that IFV has a smooth surface without any prominent protrude or depression. Comparison of the IFV structure with those of the insect picorna-like virus-Cricket paralysis virus (CrPV)and human picornavirus-Human rhinovirus 14 (HRV 14) revealed that the IFV structure resembles the CrPV structure. The "Rossmann canyon" is absent in both IFV and CrPV particles. The polypeptide topology of IFV VP2, IFV VP3 was predicted and the subunit location at the capsid surface was further analyzed.
Xie
Li
L
Institute of Biotechnology, Zhejiang University, Hangzhou, China.
Zhang
QinFen
Q
Lu
XingMeng
X
Dai
XinHong
X
Li
KunPeng
K
Hong
Jian
J
Zhou
XuePing
X
D002213:Capsid / Q000378:metabolism / Q000648:ultrastructure*; D036022:Capsid Proteins / Q000737:chemistry / Q000378:metabolism; D020285:Cryoelectron Microscopy / Q000379:methods*; D021621:Imaging, Three-Dimensional; D008958:Models, Molecular; D010849:Picornaviridae / Q000378:metabolism / Q000648:ultrastructure*; D017510:Protein Folding
D036022:Capsid Proteins