Three-dimensional visualization of tegument/capsid interactions in the intact human cytomegalovirus.
The three-dimensional structure of the intact human cytomegalovirus (HCMV) was determined to 18-A resolution by electron cryomicroscopy and computer reconstruction. Its capsid shell is composed of pentons, hexons, and triplexes arranged on a T = 16 icosahedral lattice and is identical to that of the B-capsid isolated from host cell nuclei. An icosahedrally ordered tegument layer formed by 960 copies of filamentous density is also visualized, which interacts with the pentons, hexons, and triplexes of the underlying capsid. The observed structural similarities and differences of HCMV with those of herpes simplex virus offer insights into the significance of the different tegument components for their infection processes while maintaining similar capsids.
Chen
D H
DH
Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas, 77030, USA.
Jiang
H
H
Lee
M
M
Liu
F
F
Zhou
Z H
ZH
D002213:Capsid / Q000648:ultrastructure*; D002478:Cells, Cultured; D003198:Computer Simulation; D020285:Cryoelectron Microscopy; D003587:Cytomegalovirus / Q000648:ultrastructure*; D005347:Fibroblasts / Q000821:virology; D006801:Humans; D008958:Models, Molecular