Three-Dimensional Structure of Herpes Simplex Virus from Cryo-Electron Tomography
Abstract
Herpes simplex virus, a DNA virus of high complexity, consists of a nucleocapsid surrounded by the tegument—a protein compartment—and the envelope. The latter components, essential for infectivity, are pleiomorphic. Visualized in cryo–electron tomograms of isolated virions, the tegument was seen to form an asymmetric cap: On one side, the capsid closely approached the envelope; on the other side, they were separated by ∼35 nanometers of tegument. The tegument substructure was particulate, with some short actin-like filaments. The envelope contained 600 to 750 glycoprotein spikes that varied in length, spacing, and in the angles at which they emerge from the membrane. Their distribution was nonrandom, suggesting functional clustering.
Additional Information
© 2003 American Association for the Advancement of Science. 11 August 2003; accepted 7 October 2003. We thank B. Trus, A. Frangakis, and O. Medalia for help and advice and gratefully acknowledge contributions from an Emmy Noether fellowship from the Deutsche Forschungsgemeinschaft (K.G.), a Humboldt Foundation fellowship (A.C.S.), the NIH Intramural AIDS Targeted Antiviral Program (A.C.S.), and U.S. Public Health Service grant AI33077 (P.D.) for the support of this research.Attached Files
Supplemental Material - Gruenewald.SOM.pdf
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Additional details
- Eprint ID
- 51888
- Resolver ID
- CaltechAUTHORS:20141118-094920919
- Deutsche Forschungsgemeinschaft (DFG)
- Alexander von Humboldt Foundation
- NIH
- AI33077
- U. S. Public Health Service
- Created
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2014-11-18Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field