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Structural determinants of rotavirus subgroup specificity mapped by cryo-electron microscopy

Academic Article
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Overview

authors

  • Greig, S. L.
  • Berriman, J. A.
  • O'Brien, J. A.
  • Taylor, J. A.
  • Bellamy, A. R.
  • Yeager, Mark
  • Mitra, A. K.

publication date

  • February 2006

journal

  • Journal of Molecular Biology  Journal

abstract

  • The rotavirus double-layered particle (DLP) is a molecular machine that transcribes 11 genomic segments of double-stranded RNA into full-length mRNA segments during viral replication. DLPs from the human Wa strain of virus, belonging to subgroup II (SG II), possess a significantly reduced level of transcriptase activity compared to bovine UK DLPs that belong to subgroup I (SG I). Cryo-electron microscopy and icosahedral image analysis was used to define the structural basis for this difference in transcriptase activity and to derive three-dimensional density maps of bovine UK and human Wa DLPs at 26 angstroms and 28 angstroms resolution, respectively. The two rotavirus strains had the same diameter, T = 13 l icosahedral lattice symmetry and size of the VP6 trimers on the surface of the DLPs. However, the Wa particles displayed a remarkable absence of VP6 trimers surrounding each 5-fold vertex position. To further explore these structural differences, three-dimensional reconstructions were generated of DLPs decorated with Fab fragments derived from subgroup-specific monoclonal antibodies. The X-ray structures of VP6 and a generic Fab fragment were then docked into the cryo-electron microscopy density maps, which allowed us to propose at "pseudo-atomic" resolution the locations of the amino acid residues defining the subgroup-specific epitopes. Our results demonstrate a correlation between the structure of the VP6 layer and the transcriptase activity of the particles, and suggest that the stability of VP6 trimers, specifically those at the icosahedral 5-fold axes, may be critical for mRNA synthesis. Thus, subgroup specificity of rotavirus may reflect differences in the architecture of the double-layered particle, with resultant consequences for viral mRNA synthesis.

subject areas

  • Animals
  • Antibodies, Monoclonal
  • Antibodies, Viral
  • Binding Sites
  • Cattle
  • Cryoelectron Microscopy
  • Epitopes
  • Humans
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Quaternary
  • RNA-Directed DNA Polymerase
  • Rotavirus
  • Viral Proteins
  • Virion
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Research

keywords

  • Fab fragments
  • capsid structure
  • cryo-electron microscopy
  • image analysis
  • rotavirus
  • subgroup specificity
  • transcriptase
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2005.11.049

PubMed ID

  • 16359700
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Additional Document Info

start page

  • 209

end page

  • 221

volume

  • 356

issue

  • 1

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