1887

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Volume 87, Issue 11

Identification of the cleavage sites of sapovirus open reading frame 1 polyprotein Free

Abstract

Sapovirus (SaV), a member of the family , is a causative agent of acute gastroenteritis in humans and swine and is currently divided into five genogroups, GI–GV. The proteolytic processing of the SaV open reading frame 1 (ORF1) polyprotein with a human GII SaV Mc10 strain has recently been determined and the products are arranged in the following order: NH–p11–p28–p35 (NTPase)–p32–p14 (VPg)–p70 (Pro–Pol)–p60 (VP1)–COOH. The cleavage site between p14 (VPg) and p70 (Pro–Pol) was identified as E/A by N-terminal amino acid sequencing. To identify other cleavage sites, a series of GII SaV Mc10 full-length clones containing disrupted potential cleavage sites in the ORF1 polyprotein were constructed and used to generate linear DNA templates for coupled transcription–translation. The translation products were analysed by SDS-PAGE or by immunoprecipitation with region-specific antibodies. N-terminal amino acid sequencing with -expressed recombinant proteins was also used to identify the cleavage site between p32 and p14. These approaches enabled identification of the six cleavage sites of the Mc10 ORF1 polyprotein as E/G, Q/G, Q/G, E/A, E/A and E/G. The alignment of the SaV full-length ORF1 amino acid sequences indicated that the dipeptides used for the cleavage sites were either E or Q at the P1 position and A, G or S at the P1′ position, which were conserved in the GI, GII, GIII, GIV and GV SaV ORF1 polyprotein.

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2006-11-01
2024-04-26
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References

  1. Belliot G., Sosnovtsev S. V., Mitra T., Hammer C., Garfield M., Green K. Y. 2003; In vitro proteolytic processing of the MD145 norovirus ORF1 nonstructural polyprotein yields stable precursors and products similar to those detected in calicivirus-infected cells. J Virol 77:10957–10974 [CrossRef]
     [Google Scholar]
  2. Blakeney S. J., Cahill A., Reilly P. A. 2003; Processing of Norwalk virus nonstructural proteins by a 3C-like cysteine proteinase. Virology 308:216–224 [CrossRef]
     [Google Scholar]
  3. Chang K.-O., Sosnovtsev S. V., Belliot G., Kim Y., Saif L. J., Green K. Y. 2004; Bile acids are essential for porcine enteric calicivirus replication in association with down-regulation of signal transducer and activator of transcription 1. Proc Natl Acad Sci U S A 101:8733–8738 [CrossRef]
     [Google Scholar]
  4. Chen R., Neill J. D., Noel J. S., Hutson A. M., Glass R. I., Estes M. K., Prasad B. V. V. 2004; Inter- and intragenus structural variations in caliciviruses and their functional implications. J Virol 78:6469–6479 [CrossRef]
     [Google Scholar]
  5. Clarke I. N., Lambden P. R. 2000; Organization and expression of calicivirus genes. J Infect Dis 181 (Suppl. 2):S309–S316 [CrossRef]
     [Google Scholar]
  6. Farkas T., Zhong W. M., Jing Y. & 7 other authors 2004; Genetic diversity among sapoviruses. Arch Virol 149:1309–1323
     [Google Scholar]
  7. Flynn W. T., Saif L. J. 1988; Serial propagation of porcine enteric calicivirus-like virus in primary porcine kidney cell cultures. J Clin Microbiol 26:206–212
     [Google Scholar]
  8. Green K. Y., Ando T., Balayan M. S. & 8 other authors 2000; Taxonomy of the caliciviruses. J Infect Dis 181 (Suppl. 2):S322–S330 [CrossRef]
     [Google Scholar]
  9. Guntapong R., Hansman G. S., Oka T., Ogawa S., Kageyama T., Pongsuwanna Y., Katayama K. 2004; Norovirus and sapovirus infections in Thailand. Jpn J Infect Dis 57:276–278
     [Google Scholar]
  10. Guo M., Hayes J., Cho K. O., Parwani A. V., Lucas L. M., Saif L. J. 2001a; Comparative pathogenesis of tissue culture-adapted and wild-type Cowden porcine enteric calicivirus (PEC) in gnotobiotic pigs and induction of diarrhea by intravenous inoculation of wild-type PEC. J Virol 75:9239–9251 [CrossRef]
     [Google Scholar]
  11. Guo M., Qian Y., Chang K.-O., Saif L. J. 2001b; Expression and self-assembly in baculovirus of porcine enteric calicivirus capsids into virus-like particles and their use in an enzyme-linked immunosorbent assay for antibody detection in swine. J Clin Microbiol 39:1487–1493 [CrossRef]
     [Google Scholar]
  12. Hansman G. S., Doan L. T., Kguyen T. A. & 9 other authors 2004a; Detection of norovirus and sapovirus infection among children with gastroenteritis in Ho Chi Minh City. Vietnam. Arch Virol 149:1673–1688
     [Google Scholar]
  13. Hansman G. S., Katayama K., Maneekarn N. & 7 other authors 2004b; Genetic diversity of norovirus and sapovirus in hospitalized infants with sporadic cases of acute gastroenteritis in Chiang Mai. Thailand. J Clin Microbiol 42:1305–1307 [CrossRef]
     [Google Scholar]
  14. Hansman G. S., Katayama K., Oka T., Natori K., Takeda N. 2005a; Mutational study of sapovirus expression in insect cells. Virol J 2:13 [CrossRef]
     [Google Scholar]
  15. Hansman G. S., Matsubara N., Oka T., Ogawa S., Natori K., Takeda N., Katayama K. 2005b; Deletion analysis of the sapovirus VP1 gene for the assembly of virus-like particles. Arch Virol 150:2529–2538 [CrossRef]
     [Google Scholar]
  16. Hansman G. S., Natori K., Oka T., Ogawa S., Tanaka K., Nagata N., Ushijima H., Takeda N., Katayama K. 2005c; Cross-reactivity among sapovirus recombinant capsid proteins. Arch Virol 150:21–36 [CrossRef]
     [Google Scholar]
  17. Hansman G. S., Takeda N., Oka T., Oseto M., Hedlund K. O., Katayama K. 2005d; Intergenogroup recombination in sapoviruses. Emerg Infect Dis 11:1916–1920
     [Google Scholar]
  18. Hansman G. S., Takeda N., Katayama K., Tu E. T., McIver C. J., Rawlinson W. D., White P. A. 2006; Genetic diversity of Sapovirus in children, Australia. Emerg Infect Dis 12:141–143 [CrossRef]
     [Google Scholar]
  19. Hardy M. E., Crone T. J., Brower J. E., Ettayebi K. 2002; Substrate specificity of the Norwalk virus 3C-like proteinase. Virus Res 89:29–39 [CrossRef]
     [Google Scholar]
  20. Jiang X., Zhong W., Kaplan M., Pickering L. K., Matson D. O. 1999; Expression and characterization of Sapporo-like human calicivirus capsid proteins in baculovirus. J Virol Methods 78:81–91 [CrossRef]
     [Google Scholar]
  21. Johansson P. J. H., Bergentoft K., Larsson P. A., Magnusson G., Widell A., Thorhagen M., Hedlund K.-O. 2005; A nosocomial sapovirus-associated outbreak of gastroenteritis in adults. Scand J Infect Dis 37:200–204 [CrossRef]
     [Google Scholar]
  22. Katayama K., Shirato-Horikoshi H., Kojima S. & 9 other authors 2002; Phylogenetic analysis of the complete genome of 18 Norwalk-like viruses. Virology 299:225–239 [CrossRef]
     [Google Scholar]
  23. Katayama K., Miyoshi T., Uchino K., Oka T., Tanaka T., Takeda N., Hansman G. S. 2004; Novel recombinant sapovirus. Emerg Infect Dis 10:1874–1876 [CrossRef]
     [Google Scholar]
  24. König M., Thiel H.-J., Meyers G. 1998; Detection of viral proteins after infection of cultured hepatocytes with rabbit hemorrhagic disease virus. J Virol 72:4492–4497
     [Google Scholar]
  25. Liu B., Clarke I. N., Lambden P. R. 1996; Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis. J Virol 70:2605–2610
     [Google Scholar]
  26. Liu B. L., Viljoen G. J., Clarke I. N., Lambden P. R. 1999; Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli . J Gen Virol 80:291–296
     [Google Scholar]
  27. Martin Alonso J. M., Casais R., Boga J. A., Parra F. 1996; Processing of rabbit hemorrhagic disease virus polyprotein. J Virol 70:1261–1265
     [Google Scholar]
  28. Mayo M. A. 2002; A summary of taxonomic changes recently approved by ICTV. Arch Virol 147:1655–1663 [CrossRef]
     [Google Scholar]
  29. Meyers G., Wirblich C., Thiel H.-J., Thumfart J. O. 2000; Rabbit hemorrhagic disease virus: genome organization and polyprotein processing of a calicivirus studied after transient expression of cDNA constructs. Virology 276:349–363 [CrossRef]
     [Google Scholar]
  30. Nakata S., Honma S., Numata K. K., Kogawa K., Ukae S., Morita Y., Adachi N., Chiba S. 2000; Members of the family Caliciviridae (Norwalk virus and Sapporo virus) are the most prevalent cause of gastroenteritis outbreaks among infants in Japan. J Infect Dis 181:2029–2032 [CrossRef]
     [Google Scholar]
  31. Noel J. S., Liu B. L., Humphrey C. D. & 7 other authors 1997; Parkville virus: a novel genetic variant of human calicivirus in the Sapporo virus clade, associated with an outbreak of gastroenteritis in adults. J Med Virol 52:173–178 [CrossRef]
     [Google Scholar]
  32. Numata K., Hardy M. E., Nakata S., Chiba S., Estes M. K. 1997; Molecular characterization of morphologically typical human calicivirus Sapporo. Arch Virol 142:1537–1552 [CrossRef]
     [Google Scholar]
  33. Oka T., Katayama K., Ogawa S., Hansman G. S., Kageyama T., Miyamura T., Takeda N. 2005a; Cleavage activity of the sapovirus 3C-like protease in Escherichia coli . Arch Virol 150:2539–2548 [CrossRef]
     [Google Scholar]
  34. Oka T., Katayama K., Ogawa S., Hansman G. S., Kageyama T., Ushijima H., Miyamura T., Takeda N. 2005b; Proteolytic processing of sapovirus ORF1 polyprotein. J Virol 79:7283–7290 [CrossRef]
     [Google Scholar]
  35. Oka T., Hansman G. S., Katayama K., Ogawa S., Nagata N., Miyamura T., Takeda N. 2006; Expression of sapovirus virus-like particles in mammalian cells. Arch Virol 151:399–404 [CrossRef]
     [Google Scholar]
  36. Parra F., Boga J. A., Marin M. S., Casais R. 1993; The amino terminal sequence of VP60 from rabbit hemorrhagic disease virus supports its putative subgenomic origin. Virus Res 27:219–228 [CrossRef]
     [Google Scholar]
  37. Paul A. V., Molla A., Wimmer E. 1994; Studies of a putative amphipathic helix in the N-terminus of poliovirus protein 2C. Virology 199:188–199 [CrossRef]
     [Google Scholar]
  38. Robinson S., Clarke I. N., Vipond I. B., Caul E. O., Lambden P. R. 2002; Epidemiology of human Sapporo-like caliciviruses in the South West of England: molecular characterisation of a genetically distinct isolate. J Med Virol 67:282–288 [CrossRef]
     [Google Scholar]
  39. Seah E. L., Marshall J. A., Wright P. J. 1999; Open reading frame 1 of the Norwalk-like virus Camberwell: completion of sequence and expression in mammalian cells. J Virol 73:10531–10535
     [Google Scholar]
  40. Seah E. L., Marshall J. A., Wright P. J. 2003; trans Activity of the norovirus Camberwell proteinase and cleavage of the N-terminal protein encoded by ORF1. J Virol 77:7150–7155 [CrossRef]
     [Google Scholar]
  41. Sibilia M., Boniotti M. B., Angoscini P., Capucci L., Rossi C. 1995; Two independent pathways of expression lead to self-assembly of the rabbit hemorrhagic disease virus capsid protein. J Virol 69:5812–5815
     [Google Scholar]
  42. Someya Y., Takeda N., Miyamura T. 2000; Complete nucleotide sequence of the Chiba virus genome and functional expression of the 3C-like protease in Escherichia coli . Virology 278:490–500 [CrossRef]
     [Google Scholar]
  43. Sosnovtsev S. V., Sosnovtseva S. A., Green K. Y. 1998; Cleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase. J Virol 72:3051–3059
     [Google Scholar]
  44. Sosnovtsev S. V., Garfield M., Green K. Y. 2002; Processing map and essential cleavage sites of the nonstructural polyprotein encoded by ORF1 of the feline calicivirus genome. J Virol 76:7060–7072 [CrossRef]
     [Google Scholar]
  45. Sosnovtseva S. A., Sosnovtsev S. V., Green K. Y. 1999; Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein. J Virol 73:6626–6633
     [Google Scholar]
  46. Vinjé J., Deijl H., van der Heide R., Lewis D., Hedlund K. O., Svensson L., Koopmans M. P. 2000; Molecular detection and epidemiology of Sapporo-like viruses. J Clin Microbiol 38:530–536
     [Google Scholar]
  47. Wirblich C., Sibilia M., Boniotti M. B., Rossi C., Thiel H. J., Meyers G. 1995; 3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity. J Virol 69:7159–7168
     [Google Scholar]
  48. Wirblich C., Thiel H. J., Meyers G. 1996; Genetic map of the calicivirus rabbit hemorrhagic disease virus as deduced from in vitro translation studies. J Virol 70:7974–7983
     [Google Scholar]
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Identification of the cleavage sites of sapovirus open reading frame 1 polyprotein
J. Gen. Virol. 87, 3329 (2006); https://doi.org/10.1099/vir.0.81799-0
/content/journal/jgv/10.1099/vir.0.81799-0
/content/journal/jgv/10.1099/vir.0.81799-0
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