Caliciviruses

Abstract

The Caliciviridae is a family of small, nonenveloped viruses containing a single‐stranded, plus‐sense genomic ribonucleic acid (RNA) that is polyadenylated at its 3′‐end. Most, but not all, caliciviruses have distinctive cup‐shaped depressions (L. calix, cup) on their surface, giving them their characteristic ‘Star of David’ appearance by negative‐stain electron microscopy. The calicivirus nonstructural proteins are encoded in the 5′‐end of the genomic RNA and the structural proteins in the 3′‐end. The structural proteins are translated primarily from an abundant subgenomic RNA that is transcribed from the genomic RNA. The identity of several of the nonstructural proteins was made based on amino acid sequence similarities with other virus families. The caliciviruses encode a single capsid protein that forms the outer shell of the virus particle. These viruses have a large and diverse host range and cause diseases of both human and veterinary importance.

Key Concepts:

  • Caliciviruses constitute a unique family of viruses.

  • Caliciviruses have significant genetic diversity.

  • Calicivirusesare important agents of disease in both man and animals.

Keywords: Feline calicivirus; Vesicular exanthema of swine virus; San Miguel sea lion virus; Rabbit haemorrhagic disease virus

Figure 1.

Electron micrographs of caliciviruses. (a) Negative‐stain electron micrograph of San Miguel sea lion virus serotype 4 following caesium chloride isopycnic centrifugation of virus grown in Vero cells. Bar, 57 nm. (b) Negative‐stain electron micrograph of Feline calicivirus following caesium chloride isopycnic centrifugation of virus grown in Crandell–Rees feline kidney (CRFK) cells. Bar, 67 nm. (c) Thin‐section electron micrograph of aggregate of F. calicivirus in an infected CRFK cell. Note nucleus with swollen nuclear membrane and enlarged endoplasmic reticulum. Bar, 200 nm. Copyright © US Government.

Figure 2.

Cryoelectron microscopic representations of surface structures of four caliciviruses. The structures are at approximately 22 Å resolution. All viruses are viewed from the threefold axis of symmetry. The viruses pictured are (a) rNorwalk virus, (b) rGrimsby virus, (c) rParkville and (d) SMSV4. The bar represents 100 Å. Modified from Chen et al.. Copyright © American Society for Microbiology.

Figure 3.

X‐ray crystallographic structure of SMSV4. Structure of SMSV4 viewed on the twofold axis of symmetry. The S domain is in blue, the P1 domain is in yellow and the P2 domain is in orange. The image is shown at 3.3 Å resolution. Modified from Chen et al. . Copyright © PNAS.

Figure 4.

Comparisons of genomic RNAs from the Lagovirus, Vesivirus, Norovirus and Sapovirus genera. The single line represents the genomic RNA with the genome‐linked viral protein VPg) at the 5′‐end and the poly(A) tail at the 3′‐end. The subgenomic RNAs that have been characterized are shown beneath the region for which they are equivalent in sequence. The sizes of the RNAs in kilobases (kb) are shown. The boxes above the genomic RNA represent the ORFs in different reading frames with the approximate position of the encoded and proteins. FCV, Feline calicivirus; SMSV, San Miguel sea lion virus; VESV, Vesicular exanthema of swine virus. The figure is not drawn to scale. Copyright © US Government.

Figure 5.

Sequence comparison between the 5′‐ends of the genomic and subgenomic RNAs of (a) Feline calicivirus (FCV); (b) San Miguel sea lion virus (SMSV); (c) Rabbit haemorrhagic disease virus (RHDV); and (d) Norovirus. The 5′‐terminal bases are aligned, with identical bases marked with a colon (:) and missing nucleotides indicated by a hyphen. The comparisons are FCV (CFI strain); SMSV serotype 1; RHDV and Norovirus (Southampton virus). The nucleotide numbers from the 5′‐end of the genomic RNA are indicated. The ATG initiation codon is underlined, with multiple ATGs indicated in the Norovirus sequences because the authentic start of translation is unknown. Copyright © US Government.

Figure 6.

Western immunoblot analysis of proteins extracted from Feline calicivirus (FCV)‐infected Crandell–Rees feline kidney (CRFK) cells at various times after infection. The cells were collected at the time points indicated above each lane (hours postinfection) and the proteins were extracted. The lane marked C (control) represents uninfected CRFK cells. Following electrophoresis of proteins on a sodium dodecyl sulfate–polyacrylamide gel, the proteins were blotted to nitrocellulose and probed with FCV hyperimmune serum collected from a cat that had been infected with FCV. The capsid protein is the major protein band at approximately 60 kDa. The numbers on the left represent the size markers in kilodaltons. Copyright © US Government.

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References

Alonso C, Oviedo JM, Martin‐Alonso JM et al. (1998) Programmed cell death in the pathogenesis of rabbit hemorrhagic disease. Archives of Virology 143: 321–332.

Belliot G, Sosnovtsev SV, Chang KO et al. (2005) Norovirus proteinase‐polymerase and polymerase are both active forms of RNA‐dependent RNA polymerase. Journal of Virology 79: 2393–2403.

Berke T, Golding B, Jiang X et al. (1997) Phylogenetic analysis of the caliciviruses. Journal of Medical Virology 52: 419–424.

Chang KO, George DW, Patton JB et al. (2008) Leader of the capsid protein in feline calicivirus promotes replication of Norwalk virus in cell culture. Journal of Virology 82: 9306–9317.

Chang KO, Sosnovtsev SS, Belliot G et al. (2005) Reverse genetics system for porcine enteric calicivirus, a prototype sapovirus in the Caliciviridae. Journal of Virology 79: 1409–1416.

Chen R, Neill JD, Estes MK and Prasad PVV (2006) X‐ray structure of a native calicivirus: structural insights into antigenic diversity and host specificity. Proceedings of the National Academy of Sciences of the USA 103: 8048–8053. doi_10.1073_pnas.0600421103.

Chen R, Neill JD, Noel JS et al. (2004) Inter‐ and intragenus structural variations in caliciviruses and their functional implications. Journal of Virology 78: 6469–6479. doi: 10.1128/JVI.78.12.

Estes MK and Hardy ME (1995) Norwalk virus and other enteric caliciviruses. In: Blaser MJ, Smith PD, Ravdin JI, Greenburg HB and Guerrant RL (eds) Infection of the Gastrointestinal Tract, pp. 1009–1034. New York: Raven Press.

Ettayebi K and Hardy ME (2003) Norwalk virus non‐structural protein p48 forms a complex with the SNARE regulator VAP‐A and prevents cell surface expression of vesicular stomatitis virus G protein. Journal of Virology 77: 11790–11797.

Farkas T, Zhong WM, Jing Y et al. (2004) Genetic diversity among sapoviruses. Archives of Virology 149: 1309–1323.

Flynn WT and Saif LJ (1988) Serial propagation of porcine enteric calicivirus‐like virus in primary porcine kidney cell cultures. Journal of Clinical Microbiology 26: 206–212.

Green KY, Ando T, Balayan MS et al. (2000) Taxonomy of the caliciviruses. Journal of Infectious Diseases 181(suppl 2): S322–S330.

Karst SM, Wobus CE, Lay M, Davidson J and Virgin HW (2003) STAT1‐dependent innate immunity to a Norwalk‐like virus. Science 299: 1575–1578.

Kuyumcu‐Martinez M, Belliot G, Sosnovtsev SV et al. (2004) Calicivirus 3C‐like proteinase inhibits cellular translation by cleavage of poly(A)‐binding protein. Journal of Virology 78: 8172–8182.

Makino A, Shimojima M, Miyazawa T et al. (2006) Junctional adhesion molecule is a functional receptor for feline calicivirus. Journal of Virology 80: 4482–4490.

Meyers G (2003) Translation of the minor capsid protein of a calicivirus is initiated by a novel termination‐dependent reinitiation mechanism. Journal of Biological Chemistry 278: 34051–34060.

Neill JD, Sosnovtsev SV and Green KY (2000) Recovery and altered neutralization specificities of chimeric viruses containing capsid protein domain exchanges from antigenically distinct strains of feline calicivirus. Journal of Virology 74: 1079–1084.

Prasad BV, Matson DO and Smith AW (1994) Three‐dimensional structure of calicivirus. Journal of Molecular Biology 240: 256–264.

Pringle CR (1998) Virus taxonomy – San Diego 1998. Archives of Virology 143: 1449–1459.

Rockx BH, Vennema H, Hoebe CJ, Duizer E and Koopmans MP (2005) Association of histo‐blood group antigens and susceptibility to norovirus infections. Journal of Infectious Diseases 191: 749–754.

Sosnovtsev S and Green KY (1995) RNA transcripts derived from a cloned full‐length copy of the feline calicivirus genome do not require VpG for infectivity. Virology 210: 383–390.

Sosnovtsev SV and Green KY (2000) Identification and genomic mapping of the ORF3 and VPg proteins in feline calicivirus virions. Virology 277: 193–203.

Sosnovtsev SV, Prikhod'ko EA, Belliot G, Cohen JI and Green KY (2003) Feline calicivirus replication induces apoptosis in cultured cells. Virus Research 94: 1–10.

Wei L, Huhn JS, Mory A et al. (2001) Proteinase‐polymerase precursor as the active form of feline calicivirus RNA‐dependent RNA polymerase. Journal of Virology 75: 1211–1219.

Willcocks MM, Carter MJ and Roberts LO (2004) Cleavage of eukaryotic initiation factor eIF4G and inhibition of host‐cell protein synthesis during feline calicivirus infection. Journal of General Virology 85: 1125–1130.

Wirblich C, Thiel HJ and Meyers G (1996) Genetic map of the calicivirus rabbit hemorrhagic disease virus as deduced from in vitro translation studies. Journal of Virology 70: 7974–7983.

Zheng DP, Ando T, Fankhouser RL et al. (2006) Norovirus classification and proposed strain nomenclature. Virology 346: 312–323.

Further Reading

Green KY (2007) Caliciviridae: the Noroviruses. In: Knipe DM and Howle PM (eds) Fields Virology, 5th edn, pp. 949–979. Philadelphia: Lippincott Williams and Wilkins.

Logan C, O'Leary JJ and O'sullivan N (2007) Real‐time reverse transcription PCR detection of norovirus, sapovirus and astrovirus as causative agents of acute viral gastroenteritis. Journal of Virological Methods 146: 36–44.

Lopman BA, Brown DW and Koopmans M (2002) Human caliciviruses in Europe. Journal of Clinical Virology 24: 137–160.

Ossiboff RJ, Zhou Y, Lightfoot PJ et al. (2010) Conformational changes in the capsid protein of a calicivirus upon interaction with its functional receptor. Journal of Virology 84: 5550–5564.

Radford AD, Gaskell RM and Hart CA (2004) Human norovirus infection and the lessons from animal caliciviruses. Current Opinion in Infectious Diseases 17: 471–478.

Reuter G, Zimsek‐Mijovski J, Poljsak‐Prijatelj M et al. (2009) Incidence, diversity and molecular epidemiology of sapoviruses in swine across Europe. Journal of Clinical Microbiology 48: 363–368.

Smith AW, Skilling DE, Barlough JE and Berry ES (1986) Distribution in the north Pacific Ocean, Bering Sea and Arctic Ocean of animal populations known to carry pathogenic caliciviruses. Diseases of Aquatic Organisms 2: 73–86.

Wang QH, Han MG, Cheetham S et al. (2005) Porcine noroviruses related to human noroviruses. Emerging Infectious Diseases 11: 1874–1881.

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Neill, John D(Nov 2011) Caliciviruses. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0001013.pub3]