Serine protease of pestiviruses: Determination of cleavage sites?

Journal of Virology

Volumn 71, Issue 7, 1997, Pages 5415-5422

  Tautz, Norbert ^a   Elbers, Knut ^b   Stoll, Dieter ^c   Meyers, Gregor ^d   Thiel, Heinz Jürgen ^a  

^a JUSTUS LIEBIG UNIVERSITY   (Germany)

^b BOEHRINGER INGELHEIM PHARMA GMBH AND CO KG   (Germany)

^c UNIVERSITY OF TÜBINGEN   (Germany)

^d FEDERAL RESEARCH INSTITUTE FOR ANIMAL HEALTH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

SERINE PROTEINASE;

ANIMAL CELL; ARTICLE; BINDING SITE; DNA CLEAVAGE; ENZYME ACTIVATION; GENOTYPE; NONHUMAN; OPEN READING FRAME; PESTIVIRUS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FAMILY; PROTEIN LOCALIZATION; PROTEIN PROCESSING;

EID: 0030960350     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.7.5415-5422.1997     Document Type: Article

References (59)

1. Bartenschlager, R., L. Ahlborn-Laake, J. Mous, and H. Jacobsen. 1993. Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions. J. Virol. 67:3835-3844.
2. Bartenschlager, R., L. Ahlborn-Laake, K. Yasargil, J. Mous, and H. Jacobsen. 1995. Substrate determinants for cleavage in cis and in trans by hepatitis C virus NS3 proteinase. J. Virol. 69:198-205.
3. Bazan, J. F., and R. J. Fletterick. 1989. Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses. Virology 171:637-639.
4. Becher, P., A. D. Shannon, N. Tautz, and H.-J. Thiel. 1994. Molecular characterization of border disease virus, a pestivirus from sheep. Virology 198:542-551.
5. Collett, M. S., R. Larson, S. Belzer, and E. Retzel. 1988. Proteins encoded by bovine viral diarrhea virus: the genome organization of a pestivirus. Virology 165:200-208.
6. Collett, M. S., R. Larson, C. Gold, D. Strick, D. K. Anderson, and A. F. Purchio. 1988. Molecular cloning and nucleotide sequence of the pestivirus bovine viral diarrhea virus. Virology 165:191-199.
7. Collett, M. S., V. Moennig, and M. C. Horzinek. 1989. Recent advances in pestivirus research. J. Gen. Virol. 70:253-266.
8. Collett, M. S., M. A. Wiskerchen, E. Welniak, and S. K. Belzer. 1991. Bovine viral diarrhea virus genomic organization. Arch. Virol. 3(Suppl.):19-27.
9. Conzelmann, K. K., and M. J. Schnell. 1994. Rescue of synthetic genomic RNA analogs of rabies virus by plasmid-encoded proteins. J. Virol. 68:713-719.
10. Corapi, W. V., R. O. Donis, and E. J. Dubovi. 1990. Characterization of a panel of monoclonal antibodies and their use in the study of the antigenic diversity of bovine viral diarrhea virus. Am. J. Vet. Res. 51:1388-1394.
11. Corapi, W. V., R. O. Donis, and E. J. Dubovi. 1988. Monoclonal antibody analyses of cytopathic and noncytopathic viruses from fatal bovine viral diarrhea infections. J. Virol. 62:2823-2827.
12. de Moerlooze, L., C. Lecomte, S. Brown-Shimmer, D. Schmelz, C. Guiot, D. Vandenbergh, D. Allaer, M. Rossius, G. Chappuis, D. Dina, A. Renard, and J. A. Martial. 1993. Nucleotide sequence of the bovine viral diarrhoea virus Osloss strain: comparison with related viruses and identification of specific DNA probes in the 5′ untranslated region. J. Gen. Virol. 74:1433-1438.
13. de Moerlooze, L., I. Struman, A. Renard, and J. A. Martial. 1992. Stabilization of T7-promoter-based pARHS expression vectors using the par B locus. Gene. 119:91-93.
14. Deng, R., and K. V. Brock. 1992. Molecular cloning and nucleotide sequence of a pestivirus genome, noncytopathogenic bovine viral diarrhea virus strain SD-1. Virology. 191:867-879.
15. Devereux, J., P. Haeberli, and O. A. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
16. Doucet, J.-P., and J.-M. Trifaro. 1988. A discontinuous and highly porous sodium dodecyl sulfate-polyacrylamide slab gel system of high resolution. Anal. Biochem. 168:265-271.
17. Elbers, K., N. Tautz, P. Becher, T. Rümenapf, and H.-J. Thiel. 1996. Processing in the pestivirus E2-NS2 region: identification of the nonstructural proteins p7 and E2p7. J. Virol. 70:4131-4135.
18. Failla, C., L. Tomei, and R. de Francesco. 1994. Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins. J. Virol. 68:3753-3760.
19. Fuerst, T. R., E. G. Niles, F. W. Studier, and B. Moss. 1986. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA. 83:8122-8126.
20. Gorbalenya, A. E., E. V. Koonin, A. P. Donchenko, and V. M. Blinov. 1989. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 17:4713-4729.
21. Graf, L., C. S. Craik, A. Patthy, S. Roczniak, R. J. Fletterick, and W. J. Rutter. 1987. Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin. Biochemistry 26:2616-2622.
22. Grakoui, A., D. W. McCourt, C. Wychowsky, S. Feinstone, and C. Rice. 1993. Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites. J. Virol. 67: 2832-2843.
23. Hedstrom, L., L. Szilagyi, and W. J. Rutter. 1992. Converting trypsin to chymotrypsin: the role of surface loops. Science. 255:1249-1253.
24. Hijikata, M., H. Mizushima, T. Akagi, S. Mori, N. Kakiuchi, N. Kato, T. Tanaka, K. Kimura, and K. Shimotohno. 1993. Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus. J. Virol. 67:4665-4675.
25. Kessler, S. W. 1981. Use of protein A bearing staphylococci for the immunoprecipitation and isolation of antigens from cells. Methods Enzymol. 73: 442-459.
26. Kim, J. L., K. A. Morgenstern, C. Lin, T. Fox, M. D. Dwyer, J. A. Landro, S. P. Chambers, W. Markland, C. A. Lepre, E. T. O'Malley, S. L. Harbeson, C. M. Rice, M. A. Murcko, P. R. Caron, and J. A. Thomson. 1996. Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide. Cell 87:343-355.
27. Kolykhalov, A. A., E. V. Agapov, and C. Rice. 1994. Specificity of the hepatitis C virus NS3 serine protease: effects of substitutions at the 3/4A, 4A/4B, and 5A/5B cleavage sites on polyprotein processing. J. Virol. 68:7525-7533.
28. Lin, C., B. M. Pragai, A. Grakoui, J. Xu, and C. M. Rice. 1994. Hepatitis C virus NS3 serine proteinase: trans-cleavage requirements and processing kinetics. J. Virol. 68:8147-8157.
29. Love, R. A., H. E. Parge, J. A. Wickersham, Z. Hostomsky, N. Habuka, E. W. Moomaw, T. Adachi, and Z. Hostomska. 1996. The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site. Cell 87:331-342.
30. Meyers, G., T. Rümenapf, and H.-J. Thiel. 1989. Molecular cloning and nucleotide sequence of the genome of hog cholera virus. Virology 171:555-567.
31. Meyers, G., N. Tautz, P. Becher, H.-J. Thiel, and B. Kümmerer. 1996. Recovery of cytopathogenic and noncytopathogenic bovine viral diarrhea viruses from cDNA constructs. J. Virol. 70:8606-8613.
32. Meyers, G., N. Tautz, E. J. Dubovi, and H.-J. Thiel. 1991. Viral cytopathogenicity correlated with integration of ubiquitin-coding sequences. Virology 180:602-616.
33. Meyers, G., N. Tautz, R. Stark, J. Brownlie, E. J. Dubovi, M. S. Collett, and H.-J. Thiel. 1992. Rearrangement of viral sequences in cytopathogenic pestiviruses. Virology 191:368-386.
34. Meyers, G., and H.-J. Thiel. 1995. Cytopathogenicity of classical swine lever virus caused by defective interfering particles. J. Virol. 69:3683-3689.
35. Meyers, G., H.-J. Thiel, and T. Rümenapf. 1996. Classical swine fever virus: recovery of infectious viruses from cDNA constructs and generation of recombinant cytopathogenic defective interfering particles. J. Virol. 70:1588-1595.
36. Moormann, R. J. M., H. G. P. van Gennip, G. K. W. Miedema, M. M. Hulst, and P. A. van Rijn. 1996. Infectious RNA transcribed from an engineered full-length cDNA template of the genome of a pestivirus. J. Virol. 70:763-770.
37. Moormann, R. J. M., P. A. M. Warmerdam, B. Van der Meer, W. M. M. Schaaper, G. Wensvoort, and M. M. Hulst. 1990. Molecular cloning and nucleotide sequence of hog cholera virus strain brescia and mapping of the genomic region encoding envelope glycoprotein E1. Virology 177:184-198.
38. Pocock, D. H., C. J. Howard, M. C. Clarke, and J. Brownlie. 1987. Variation in the intracellular polypeptide profiles from different isolates of bovine viral diarrhea virus. Arch. Virol. 94:43-53.
39. Purchio, A. F., R. Larson, and M. S. Collett. 1984. Characterization of bovine viral diarrhea viral proteins. J. Virol. 50:666-669.
40. Renard, A., D. Dino, and J. Martial. 1987. Vaccines and diagnostics derived from bovine diarrhea virus. European patent application number 86870095.6, publication number 02.08672.
41. Rice, C. M. 1996. Flaviviridae: the viruses and their replication, p. 931-959. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed., vol. 1. Lippincott-Raven Publishers, Philadelphia, Pa.
42. Ridpath, J. F., and S. R. Bolin. 1995. The genomic sequence of a virulent bovine viral diarrhea virus (BVDV) from the type 2 genotype: detection of a large genomic insertion in a noncytopathic BVDV. Virology 212:39-46.
43. Ruggli, N., J.-D. Tratschin, C. Mittelholzer, and M. A. Hofmann. 1996. Nucleotide sequence of classical swine fever virus strain Alfort/187 and transcription of infectious RNA from stably cloned full-length cDNA. J. Virol. 70:3478-3487.
44. Rümenapf, T., G. Unger, J. H. Strauss, and H.-J. Thiel. 1993. Processing of the envelope glycoproteins of pestiviruses. J. Virol. 67:3288-3295.
45. Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
46. Stark, R., G. Meyers, T. Rümenapf, and H.-J. Thiel. 1993. Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus. J. Virol. 67:7088-7095.
47. Studier, F. W., and B. A. Moffatt. 1986. Use of the T7 bacteriophage RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
48. Suzich, J. A., J. K. Tamura, F. Palmer-Hill, P. Warrener, A. Grakoui, C. M. Rice, S. M. Feinstone, and M. S. Collett. 1993. Hepatitis C virus NS3 protein polynucleotide-stimulated nucleoside triphosphatase and comparison with the related pestivirus and flavivirus enzymes. J. Virol. 67:6152-6158.
49. Tamura, J. K., P. Warrener, and M. S. Collett. 1993. RNA-stimulated NTPase activity associated with the p80 protein of the pestivirus bovine viral diarrhea virus. Virology 193:1-10.
50. 49a. Tautz, N., et al. Unpublished data.
51. Tautz, N., G. Meyers, R. Stark, E. J. Dubovi, and H.-J. Thiel. 1996. Cytopathogenicity of a pestivirus correlated with a 27-nucleotide insertion. J. Virol. 70:7851-7858.
52. Tautz, N., G. Meyers, and H.-J. Thiel. 1993. Processing of poly-ubiquitin in the polyprotein of an RNA virus. Virology 197:74-85.
53. Tautz, N., H.-J. Thiel, E. J. Dubovi, and G. Meyers. 1994. Pathogenesis of mucosal disease: a cytopathogenic pestivirus generated by internal deletion. J. Virol. 68:3289-3297.
54. Thiel, H.-J., P. G. W. Plagemann, and V. Moennig. 1996. Pestiviruses, p. 1059-1073. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed., vol. 1. Lippincott-Raven Publishers, Philadelphia, Pa.
55. Thiel, H.-J., R. Stark, E. Weiland, T. Rümenapf, and G. Meyers. 1991. Hog cholera virus: molecular composition of virions from a pestivirus. J. Virol. 65:4705-4712.
56. Vanderheijden, N., L. de Moerlooze, D. Vanderbergh, G. Chappuis, A. Renard, and C. Lecompte. 1993. Expression of the bovine viral diarrhoea virus Osloss p80 protein: its use as ELISA antigen for cattle serum antibody detection. J. Gen. Virol. 74:1427-1431.
57. Venekei, I., L. Szilagyi, L. Graf, and W. J. Rutter. 1996. Attempts to convert chymotrypsin to trypsin. FEBS Lett. 379:143-147.
58. Warrener, P., and M. S. Collett. 1995. Pestivirus NS3 (p80) protein possesses RNA helicase activity. J. Virol. 69:1720-1726.
59. Wiskerchen, M. A., and M. S. Collett. 1991. Pestivirus gene expression: protein p80 of bovine viral diarrhea virus is a proteinase involved in polyprotein processing. Virology 184:341-350.