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

Kay Grünewald; Prashant Desai; Dennis C. Winkler; J. Bernard Heymann; David M. Belnap; Wolfgang Baumeister; Alasdair C. Steven

doi:10.1126/science.1090284

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

Kay Grünewald, Prashant Desai, Dennis C. Winkler, J. Bernard Heymann, David M. Belnap, Wolfgang Baumeister, Alasdair C. Steven

School of Medicine

Research output: Contribution to journal › Article › peer-review

412 Scopus citations

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.

Original language	English (US)
Pages (from-to)	1396-1398
Number of pages	3
Journal	Science
Volume	302
Issue number	5649
DOIs	https://doi.org/10.1126/science.1090284
State	Published - Nov 21 2003

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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.",

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AU - Grünewald, Kay

AU - Desai, Prashant

AU - Winkler, Dennis C.

AU - Heymann, J. Bernard

AU - Belnap, David M.

AU - Baumeister, Wolfgang

AU - Steven, Alasdair C.

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

Abstract

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