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Science 21 November 2003:
Vol. 302. no. 5649, pp. 1396 - 1398
DOI: 10.1126/science.1090284
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Reports

Three-Dimensional Structure of Herpes Simplex Virus from Cryo-Electron Tomography

Kay Grünewald,1 Prashant Desai,2 Dennis C. Winkler,1 J. Bernard Heymann,1,3 David M. Belnap,1 Wolfgang Baumeister,4 Alasdair C. Steven1*

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.

1 Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
2 Department of Pharmacology and Molecular Sciences, Johns Hopkins University, Baltimore, MD 21205, USA.
3 Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.
4 Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.

* To whom correspondence should be addressed. E-mail: Alasdair_Steven{at}nih.gov

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