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Science 8 October 1999: Vol. 286. no. 5438, pp. 287 - 290 DOI: 10.1126/science.286.5438.287
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Reports
X-ray Crystallographic Structure of the Norwalk Virus Capsid
B. V. V. Prasad,
1*
Michele E. Hardy,
2
Terje Dokland,
3
Jordi Bella,
3
Michael G. Rossmann,
3
Mary K. Estes
2
Norwalk virus, a noncultivatable human calicivirus, is the major
cause of epidemic gastroenteritis in humans. The first x-ray structure
of a calicivirus capsid, which consists of 180 copies of a single
protein, has been determined by phase extension from a low-resolution
electron microscopy structure. The capsid protein has a protruding (P)
domain connected by a flexible hinge to a shell (S) domain that has a
classical eight-stranded -sandwich motif. The structure of the P
domain is unlike that of any other viral protein with a subdomain
exhibiting a fold similar to that of the second domain in the
eukaryotic translation elongation factor-Tu. This subdomain, located
at the exterior of the capsid, has the largest sequence variation among
Norwalk-like human caliciviruses and is likely to contain the
determinants of strain specificity and cell binding.
1 Verna and Marrs Mclean Department of
Biochemistry,
2 Division of Molecular Virology,
Baylor College of Medicine, Houston, TX 77030, USA.
3 Department of Life Sciences, Purdue University,
West Lafayette, IN 47907, USA.
*
To whom correspondence should be addressed. E-mail:
vprasad{at}bcm.tmc.edu
Present address: Veterinary Molecular Biology, Montana
State University, Bozeman, MT 59717, USA.
Present address: Institute of Molecular Agrobiology,
National University of Singapore, Singapore 117604.
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77, 13117-13124
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