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Journal of Virology, June 2004, p. 6469-6479, Vol. 78, No. 12
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.12.6469-6479.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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

Rong Chen,1 John D. Neill,2 Jacqueline S. Noel,3 Anne M. Hutson,4 Roger I. Glass,3 Mary K. Estes,4 and B. V. Venkataram Prasad1*

Verna and Marrs McLean Department of Biochemistry and Molecular Biology,1 Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas 77030,4 National Animal Disease Center, Agriculture Research Service, U.S. Department of Agriculture, Ames, Iowa 50010,2 Viral Gastroenteritis Unit, Division of Viral and Rickettsial Diseases, National Center for Infectious Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia 303333

Received 9 September 2003/ Accepted 5 February 2004

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.

* Corresponding author. Mailing address: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Alkek Building N410, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030. Phone: (713) 798-5686. Fax: (713) 798-1625. E-mail: vprasad{at}bcm.tmc.edu.

Journal of Virology, June 2004, p. 6469-6479, Vol. 78, No. 12
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.12.6469-6479.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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