Hostname: page-component-586b7cd67f-t7fkt Total loading time: 0 Render date: 2024-12-01T04:07:23.900Z Has data issue: false hasContentIssue false

Cytomegalovirus Capsid Structure and Tegument Binding

Published online by Cambridge University Press:  02 July 2020

A. C. Steven
Affiliation:
Laboratory of Structural Biology, NIAMS Engineering Laboratory, DCRT, National Institutes of Health, Bethesda, MD20892
W. Gibson
Affiliation:
Virology Laboratories, Johns Hopkins School of Medicine, Baltimore, MD21205
N. Cheng
Affiliation:
Laboratory of Structural Biology, NIAMS Engineering Laboratory, DCRT, National Institutes of Health, Bethesda, MD20892
B. L. Trus
Affiliation:
Laboratory of Structural Biology, NIAMS Engineering Laboratory, DCRT, National Institutes of Health, Bethesda, MD20892 Computational Bioscience and Engineering Laboratory, DCRT, National Institutes of Health, Bethesda, MD20892
Get access

Extract

Herpesviruses form an extensive family of DNA viruses, in which three subfamilies called alpha-, beta- and gammaherpesviruses, respectively, are distinguished on the basis of biological properties. In terms of overall structure, all herpesviruses conform to a common plan: the virion consists of a thick-walled capsid, ∼ 1250 Å in diameter, containing the genome, surrounded by a complex layer of proteins called the tegument (a feature unique to herpesviruses), and a lipoprotein envelope. At a more detailed level, it has not been clear whether the three subfamilies are also differentiated structurally. The molecular architecture of alphaherpesvirus capsids has been studied by cryoelectron microscopy of herpes simplex virus 1, revealing its icosahedral (T=16) surface lattice and the locations of the four abundant shell proteins. To ascertain how closely these features are emulated in a betaherpesvirus, we have studied capsids of simian cytomegalovirus (SCMV) by similar methods. By comparing the structures of nuclear capsids and cytoplasmic capsids (which have bound some tegument proteins),

Type
Chambers and Channels: Functional Connections in Multiprotein Complexes Studied by Single Chambers and Channels
Copyright
Copyright © Microscopy Society of America

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

References:

1.Steven, A. C. & Spear, P. G., in Chiu, W. et al, Eds Structural Biology of Viruses, OUP (1997)312.Google Scholar
2.Newcomb, W. W. et al., J. Mol. Biol. 232(1993)499.CrossRefGoogle Scholar
3.Baker, T. S. & Cheng, R. H., J. Struct. Biol. 116(1996)120.CrossRefGoogle Scholar
4.Gibson, W., Intervirology 39(1996)389.CrossRefGoogle Scholar