Three-dimensional structure of rotavirus

J Mol Biol. 1988 Jan 20;199(2):269-75. doi: 10.1016/0022-2836(88)90313-0.


The three-dimensional structures of double and single-shelled simian rotavirus have been determined to a resolution of 40 A by image processing electron micrographs of unstained, unfixed virus particles embedded in vitreous ice. This study demonstrates that the icosahedral surface lattices in these structures have a triangulation number of 13 in a left-handed configuration. The double-shelled virion has a smooth outer surface with 60 slender spikes. The single-shelled virion, in contrast, exhibits a bristly surface. On the basis of these structures, the locations and number of copies of outer and inner shell proteins have been deduced. The spikes likely correspond to VP3, a hemagglutinin, while the rest of the mass density in the outer shell represents 780 molecules of VP7, a neutralization antigen. The 260 morphological units, located on all the local and strict 3-fold axes of the single-shelled virion are proposed to represent 260 trimers of VP6, which is a subgroup antigen. The regions of closed contact between the outer and the inner shells are located mainly near the local and strict 3-fold axes. A distinctive feature in the rotavirus structure is the presence of 132 large channels spanning across both the shells at all 5 and 6-co-ordinated positions linking the outermost surface with the inner core. In the transcriptionally active single-shelled virion, these channels may provide pathways for importing the metabolites required for the viral RNA transcription and exporting the newly synthesized RNA molecules for subsequent viral replication processes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Capsid
  • Microscopy, Electron
  • Rotavirus / ultrastructure*
  • Viral Proteins
  • Viral Structural Proteins


  • Viral Proteins
  • Viral Structural Proteins