Visualization of Tegument-Capsid Interactions and DNA in Intact Herpes Simplex Virus Type 1 Virions
@article{Zhou1999VisualizationOT, title={Visualization of Tegument-Capsid Interactions and DNA in Intact Herpes Simplex Virus Type 1 Virions}, author={Z. Hong Zhou and Dong-Hua Chen and Joanita Jakana and Frazer J. Rixon and Wah Chiu}, journal={Journal of Virology}, year={1999}, volume={73}, pages={3210 - 3218} }
ABSTRACT Herpes simplex virus type 1 virions were examined by electron cryomicroscopy, allowing the three-dimensional structure of the infectious particle to be visualized for the first time. The capsid shell is identical to that of B-capsids purified from the host cell nucleus, with the exception of the penton channel, which is closed. The double-stranded DNA genome is organized as regularly spaced (∼26 Å) concentric layers inside the capsid. This pattern suggests a spool model for DNA…
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References
SHOWING 1-10 OF 55 REFERENCES
Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids
- BiologyNature Structural Biology
- 1995
Using 400 kV electron cryomicroscopy and computer reconstruction, the three-dimensional structures of the wild-type capsid and a recombinant baculovirus-generated HSV-1 capsid are determined and a mechanism for VP26 assembly is proposed which would account for its distribution.
Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: structural authenticity and localization of VP26
- BiologyJournal of virology
- 1995
By comparing capsids assembled with and without the expression of gene UL35, it is confirmed the presence of six copies of its product, VP26, around each hexon tip, indicating that the conformational differences between the hexon and penton states of the major capsid protein, VP5, extend to the VP26 binding site.
Identification of the sites of interaction between the scaffold and outer shell in herpes simplex virus-1 capsids by difference electron imaging.
- Biology, ChemistryProceedings of the National Academy of Sciences of the United States of America
- 1998
This work has used electron cryomicroscopy and computer image processing to determine the three-dimensional structures of capsids containing either cleaved or uncleaved scaffolding proteins and proposed that rods are formed by the C-termini of the scaffoldingprotein and represent the sites of interaction between the capsid shell and scaffold.
Microtubule-mediated Transport of Incoming Herpes Simplex Virus 1 Capsids to the Nucleus
- BiologyThe Journal of cell biology
- 1997
It was shown that the cytosolic capsid transport in Vero cells was mediated by microtubules and the attachment of dynein, a minus end–directed, microtubule-dependent motor, to the viral capsids.
Overexpression of the herpes simplex virus type 1 tegument protein VP22 increases its incorporation into virus particles.
- BiologyVirology
- 1996
Results provide the first evidence that, for certain proteins, the level of polypeptide synthesis can act as a controlling factor for the amount of protein incorporated into tegument.
Induced extrusion of DNA from the capsid of herpes simplex virus type 1
- BiologyJournal of virology
- 1994
The ability of GuHCl to cause loss of DNA from C capsids with no accompanying change in capsid morphology or protein composition suggests that penton sites may open transiently to permit DNA exist and then return to their original state.
Proteins Specified by Herpes Simplex Virus VIII. Characterization and Composition of Multiple Capsid Forms of Subtypes 1 and 2
- BiologyJournal of virology
- 1972
Two classes of herpesvirus capsids were isolated from the nuclei of human cells infected with herpes simplex virus (HSV) and the capsid proteins of HSV-1 cannot be differentiated from theirHSV-2 counterparts with respect to electrophoretic mobility.
Morphological components of herpesvirus. IV. Ultrastructural features of the envelope and tegument.
- BiologyJournal of ultrastructure research
- 1982
The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly.
- BiologyJournal of molecular biology
- 1996