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Cited by 154Viral gastroenteritis research and epidemiologyEnzyme Structure and FunctionVirology and Viral Diseases

Inter- and Intragenus Structural Variations in Caliciviruses and Their Functional Implications

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Chen, Rong, Neill, John D., Noel, Jacqueline S., Hutson, Anne M., Glass, Roger I., Estes, Mary K., Prasad, B. V. Venkataram·2004·Journal of Virology
DOI 10.1128/jvi.78.12.6469-6479.2004PMC PMC416503
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Abstract

The family Caliciviridae is divided into four genera and consists of single-stranded RNA viruses with hosts ranging from humans to a wide variety of animals. Human caliciviruses are the major cause of outbreaks of acute nonbacterial gastroenteritis, whereas animal caliciviruses cause various host-dependent illnesses with a documented potential for zoonoses. To investigate inter- and intragenus structural variations and to provide a better understanding of the structural basis of host specificity and strain diversity, we performed structural studies of the recombinant capsid of Grimsby virus, the recombinant capsid of Parkville virus, and San Miguel sea lion virus serotype 4 (SMSV4), which are representative of the genera Norovirus (genogroup 2), Sapovirus , and Vesivirus , respectively. A comparative analysis of these structures was performed with that of the recombinant capsid of Norwalk virus, a prototype member of Norovirus genogroup 1. Although these capsids share a common architectural framework of 90 dimers of the capsid protein arranged on a T=3 icosahedral lattice with a modular domain organization of the subunit consisting of a shell (S) domain and a protrusion (P) domain, they exhibit distinct differences. The distally located P2 subdomain of P shows the most prominent differences both in shape and in size, in accordance with the observed sequence variability. Another major difference is in the relative orientation between the S and P domains, particularly between those of noroviruses and other caliciviruses. Despite being a human pathogen, the Parkville virus capsid shows more structural similarity to SMSV4, an animal calicivirus, suggesting a closer relationship between sapoviruses and animal caliciviruses. These comparative structural studies of caliciviruses provide a functional rationale for the unique modular domain organization of the capsid protein with an embedded flexibility reminiscent of an antibody structure. The highly conserved S domain functions to provide an icosahedral scaffold; the hypervariable P2 subdomain may function as a replaceable module to confer host specificity and strain diversity; and the P1 subdomain, located between S and P2, provides additional fine-tuning to position the P2 subdomain.

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Authors
Chen, R., Neill, J. D., Noel, J. S., Hutson, A. M., Glass, R. I., Estes, M. K., & Prasad, B. V. V.
Affiliations
  • Baylor College of Medicine (US)
  • National Animal Disease Center (US)
  • Centers for Disease Control and Prevention (US)
  • Verna and Marrs McLean Department of Biochemistry and Molecular Biology
ORCID
Venue
Journal of Virology
Publisher
American Society for Microbiology
Published
2004-06-15
Volume
78
Issue
12
Pages
6469-6479
ISSN
  • 0022-538X (ISSN-L)
  • 1098-5514
DOI
10.1128/jvi.78.12.6469-6479.2004
PMC
PMC416503
OpenAlex
W2042000843
Cited by
154
References
0
Citations by year
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FWCI
6.60
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Journal of Virology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Cancer Institute (CA-09197, T32CA009197)
  • National Institute of Allergy and Infectious Diseases (R01AI38036)
Topics
  • Health Sciences › Medicine › Infectious Diseases › Viral gastroenteritis research and epidemiology
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
Keywords
Caliciviridae, norovirus, sapovirus, Vesivirus, Norwalk virus, host specificity, strain diversity, zoonoses, icosahedral lattice, single-stranded RNA viruses
MeSH terms
Amino Acid Sequence, Animals, Caliciviridae, Capsid, Crystallization, Humans, Models, Molecular, Molecular Sequence Data, Recombinant Proteins, Species Specificity, Genetic Variation, Virion, Crystallography, X-Ray, Cryoelectron Microscopy, Norovirus, Sapovirus, Vesivirus, Capsid Proteins

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