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Nature 317, 145-153 (12 September 1985) | doi:10.1038/317145a0; Accepted 30 July 1985

Structure of a human common cold virus and functional relationship to other picornaviruses

Michael G. Rossmann*, Edward Arnold*, John W. Erickson*, †, Elizabeth A. Frankenberger*, †, James P. Griffith*, Hans-Jürgen Hecht*, †, John E. Johnson*, Greg Kamer*, Ming Luo*, Anne G. Mosser‡, Roland R. Rueckert‡, Barbara Sherry‡ & Gerrit Vriend*

  1. *Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA
  2. ‡Biophysics Lab, University of Wisconsin, 1525 Linden Drive, Madison, Wisconsin 53706, USA
  3. †Present addresses: Department of Physical Biochemistry, AP-9A D-47E, Abbott Laboratories, Abbott Park, North Chicago, Illinois 60064, USA (J.W.E.); Department of Agronomy, Purdue University, West Lafayette, Indiana 47907, USA (E.A.F.) ; F. G. Roentgenstrukturanalyse, Universitaet Wuerzburg, Zentralbau Chemie, Am Hubland, D-8700 Wuerzburg, FRG (H.-J.H.).
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We report the first atomic resolution structure of an animal virus, human rhinovirus 14. It is strikingly similar to known icosahedral plant RNA viruses. Four neutralizing immunogenic regions have been identified. These, and corresponding antigenic sequences of polio and foot-and-mouth disease viruses, reside on external protrusions. A large cleft on each icosahedral face is probably the host cell receptor binding site.