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The structure of cucumber mosaic virus: Cryoelectron microscopy, x-ray crystallography, and sequence analysis

Academic Article
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Overview

authors

  • Wikoff, W. R.
  • Tsai, C. J.
  • Wang, G. J.
  • Baker, T. S.
  • Johnson Jr., John

publication date

  • May 1997

journal

  • Virology  Journal

abstract

  • The three-dimensional structure of cucumber mosaic virus (CMV) was analyzed at 23 A resolution by cryoelectron microscopy and image reconstruction, demonstrating structural similarity to cowpea chlorotic mottle virus (CCMV), another member of the Bromoviridae family. The CMV structure was determined at 8 A resolution by X-ray crystallography with phases determined by single isomorphous replacement and refined by fivefold noncrystallographic symmetry averaging. The X-ray structure agreed with the electron microscopy reconstruction; the electron density is consistent with beta-barrel subunits arranged with T = 3 quasi-symmetry in an orientation similar to that observed in CCMV. Strong density surrounding the icosahedral threefold axes (quasi sixfold axes in the T = 3 particle) between 80 and 100 A from the particle center formed a cylinder of radius 11 A, similar to the density observed in the same region of CCMV. This density corresponds to the beta-annulus of CCMV, which differentiates hexamers from pentamers and determines the formation of the T = 3 particles. The CMV and CCMV amino acid sequences were aligned, providing information (based on the CCMV atomic model) about the probable distribution of residues in the three-dimensional structure of CMV.

subject areas

  • Amino Acid Sequence
  • Capsid
  • Crystallography, X-Ray
  • Cucumis sativus
  • Cucumovirus
  • Microscopy, Electron
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
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Identity

International Standard Serial Number (ISSN)

  • 0042-6822

Digital Object Identifier (DOI)

  • 10.1006/viro.1997.8543

PubMed ID

  • 9185592
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Additional Document Info

start page

  • 91

end page

  • 97

volume

  • 232

issue

  • 1

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