Structural Studies on Gastroenteritis Viruses

  1. Derek Chadwick and
  2. Jamie A. Goode
  1. B. V. Venkataram Prasad1,
  2. S. Crawford2,
  3. J. A. Lawton1,
  4. J. Pesavento1,
  5. M. Hardy2 and
  6. M. K. Estes2

Published Online: 7 OCT 2008

DOI: 10.1002/0470846534.ch3

Gastroenteritis Viruses: Novartis Foundation Symposium 238

Gastroenteritis Viruses: Novartis Foundation Symposium 238

How to Cite

Venkataram Prasad, B. V., Crawford, S., Lawton, J. A., Pesavento, J., Hardy, M. and Estes, M. K. (2001) Structural Studies on Gastroenteritis Viruses, in Gastroenteritis Viruses: Novartis Foundation Symposium 238 (eds D. Chadwick and J. A. Goode), John Wiley & Sons, Ltd, Chichester, UK. doi: 10.1002/0470846534.ch3

Author Information

  1. 1

    Verna and Maars McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA

  2. 2

    Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX, USA

Publication History

  1. Published Online: 7 OCT 2008
  2. Published Print: 16 MAY 2001

Book Series:

  1. Novartis Foundation Symposia

Book Series Editors:

  1. Novartis Foundation

ISBN Information

Print ISBN: 9780471496632

Online ISBN: 9780470846537

SEARCH

Keywords:

  • structure;
  • gastroenteritis;
  • viruses;
  • rotavirus;
  • dsRNA;
  • Norwalk;
  • capsid;
  • X-ray structure;
  • cryoelectron microscopy;
  • VP1;
  • VP2;
  • VP3;
  • VP4;
  • VP6;
  • VP7;
  • double-layered particle

Summary

There are many recent advances in our understanding of the structure-function relationships in rotavirus, a major pathogen of infantile gastroenteritis, and Norwalk virus, a causative agent of epidemic gastroenteritis in humans. Rotavirus is a large (1000 Å) and complex icosahedral assembly formed by three concentric capsid layers that enclose the viral genome of 11 dsRNA segments. Because of its medical relevance, intriguing structural complexity, and several unique strategies in the morphogenesis and replication, this virus has been the subject of extensive biochemical, genetic and structural studies. Using a combination of electron cryomicroscopy and computer image processing together with atomic resolution X-ray structural information, we have been able to provide not only a better description of the rotavirus architecture, but also a better understanding of the structural basis of various biological functions such as trypsinenhanced infectivity, virus assembly and the dynamic process of endogenous transcription. In contrast to rotavirus, Norwalk virus has a simple architecture with an icosahedral capsid made of 180 copies of a single protein. We have determined the structure of the Norwalk virus capsid to a resolution of 3.4 Å using X-ray crystallographic techniques. These studies have provided valuable information on domain organization in the capsid protein, and residues that may be critical for dimerization, assembly, strain-specificity and antigenicity.