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Volumn 72, Issue 5, 1998, Pages 4139-4148

Insertion of a sequence encoding light chain 3 of microtubule- associated proteins 1A and 1B in a pestivirus genome: Connection with virus cytopathogenicity and induction of lethal disease in cattle

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; MICROTUBULE ASSOCIATED PROTEIN 1; VIRUS PROTEIN;

EID: 0031958596     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.5.4139-4148.1998     Document Type: Article
Times cited : (64)

References (50)
  • 1
    • 0024372153 scopus 로고
    • Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses
    • Bazan, J. F., and R. J. Fletterick. 1989. Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses. Virology 171:637-639.
    • (1989) Virology , vol.171 , pp. 637-639
    • Bazan, J.F.1    Fletterick, R.J.2
  • 2
    • 0029876718 scopus 로고    scopus 로고
    • Cytopathogenicity of border disease virus is correlated with integration of cellular sequences into the viral genome
    • Becher, P., G. Meyers, A. D. Shannon, and H.-J. Thiel. 1996. Cytopathogenicity of border disease virus is correlated with integration of cellular sequences into the viral genome. J. Virol. 70:2992-2998.
    • (1996) J. Virol. , vol.70 , pp. 2992-2998
    • Becher, P.1    Meyers, G.2    Shannon, A.D.3    Thiel, H.-J.4
  • 3
    • 0028035957 scopus 로고
    • Molecular studies of genetic RNA-RNA recombination in brome mosaic virus
    • Bujarski, J. J., P. D. Nagy, and S. Flasinski. 1994. Molecular studies of genetic RNA-RNA recombination in brome mosaic virus. Adv. Virus Res. 43:275-302.
    • (1994) Adv. Virus Res. , vol.43 , pp. 275-302
    • Bujarski, J.J.1    Nagy, P.D.2    Flasinski, S.3
  • 4
    • 0024043662 scopus 로고
    • Proteins encoded by bovine viral diarrhea virus: The genomic organization of a pestivirus
    • Collett, M. S., R. Larson, S. K. Belzer, and E. Retzel. 1988. Proteins encoded by bovine viral diarrhea virus: the genomic organization of a pestivirus. Virology 165:200-208.
    • (1988) Virology , vol.165 , pp. 200-208
    • Collett, M.S.1    Larson, R.2    Belzer, S.K.3    Retzel, E.4
  • 5
    • 0024041479 scopus 로고
    • Molecular cloning and nucleotide sequence of the pestivirus bovine viral diarrhea virus
    • 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.
    • (1988) Virology , vol.165 , pp. 191-199
    • Collett, M.S.1    Larson, R.2    Gold, C.3    Strick, D.4    Anderson, D.K.5    Purchio, A.F.6
  • 7
    • 0023783496 scopus 로고
    • Monoclonal antibody analyses of cytopathic and noncytopathic viruses from fatal bovine viral diarrhea virus infections
    • Corapi, W. V., R. O. Donis, and E. J. Dubovi. 1988. Monoclonal antibody analyses of cytopathic and noncytopathic viruses from fatal bovine viral diarrhea virus infections. J. Virol. 62:2823-2827.
    • (1988) J. Virol. , vol.62 , pp. 2823-2827
    • Corapi, W.V.1    Donis, R.O.2    Dubovi, E.J.3
  • 8
    • 0027077918 scopus 로고
    • Molecular cloning and nucleotide sequence of a pestivirus genome, noncytopathogenic bovine viral diarrhea virus strain SD-1
    • Deng, R., and K. Brock. 1992. Molecular cloning and nucleotide sequence of a pestivirus genome, noncytopathogenic bovine viral diarrhea virus strain SD-1. Virology 191:867-879.
    • (1992) Virology , vol.191 , pp. 867-879
    • Deng, R.1    Brock, K.2
  • 9
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 10
    • 0023953666 scopus 로고
    • A discontinuous and highly porous sodium dodecyl sulfate-polyacrylamide slab gel system of high resolution
    • 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.
    • (1988) Anal. Biochem. , vol.168 , pp. 265-271
    • Doucet, J.-P.1    Trifaro, J.-M.2
  • 11
    • 0029893139 scopus 로고    scopus 로고
    • Processing in the pestivirus E2-NS2 region: Identification of proteins p7 and E2p7
    • Elbers, K., N. Tautz, P. Becher, D. Stoll, T. Rümenapf, and H.-J. Thiel. 1996. Processing in the pestivirus E2-NS2 region: identification of proteins p7 and E2p7. J. Virol. 70:4131-4135.
    • (1996) J. Virol. , vol.70 , pp. 4131-4135
    • Elbers, K.1    Tautz, N.2    Becher, P.3    Stoll, D.4    Rümenapf, T.5    Thiel, H.-J.6
  • 12
    • 0000233999 scopus 로고
    • Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • 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.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 13
    • 0024341494 scopus 로고
    • N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases
    • Gorbalenya, A. E., A. P. Donchenko, E. V. Koonin, and V. M. Blinov. 1989. N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases. Nucleic Acids Res. 17:3889-3897.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 3889-3897
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Koonin, E.V.3    Blinov, V.M.4
  • 14
    • 0027122423 scopus 로고
    • Mucosal disease in cattle housed in isolation
    • Gunn, M., and E. Weavers. 1992. Mucosal disease in cattle housed in isolation. Vet. Rec. 131:376.
    • (1992) Vet. Rec. , vol.131 , pp. 376
    • Gunn, M.1    Weavers, E.2
  • 15
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual, p. 460. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1988) Antibodies: A Laboratory Manual , pp. 460
    • Harlow, E.1    Lane, D.2
  • 16
    • 0023484188 scopus 로고
    • Unidirectional digestion with exonuclease III in DNA sequence analysis
    • Henikoff, S. 1987. Unidirectional digestion with exonuclease III in DNA sequence analysis. Methods Enzymol. 155:156-165.
    • (1987) Methods Enzymol. , vol.155 , pp. 156-165
    • Henikoff, S.1
  • 17
    • 0025801332 scopus 로고
    • The polymerase in its labyrinth: Mechanisms and implications of RNA recombination
    • Jarvis, T. C., and K. Kirkegaard. 1991. The polymerase in its labyrinth: mechanisms and implications of RNA recombination. Trends Genet. 7: 186-191.
    • (1991) Trends Genet. , vol.7 , pp. 186-191
    • Jarvis, T.C.1    Kirkegaard, K.2
  • 18
    • 0019739813 scopus 로고
    • Use of protein A-bearing staphylococci for the immunoprecipitation and isolation of antigens from cells
    • Kessler, S. W. 1981. Use of protein A-bearing staphylococci for the immunoprecipitation and isolation of antigens from cells. Methods Enzymol. 73: 442-459.
    • (1981) Methods Enzymol. , vol.73 , pp. 442-459
    • Kessler, S.W.1
  • 19
    • 0007786455 scopus 로고
    • Genetic recombination in RNA viruses
    • D. J. Rowlands, M. A. Mayo, and B. W. J. Mahy (ed.). Academic Press, London, United Kingdom
    • King, A. M. Q., S. A. Ortlepp, J. W. I. Newman, and D. McCahon. 1987. Genetic recombination in RNA viruses, p. 129-152. In D. J. Rowlands, M. A. Mayo, and B. W. J. Mahy (ed.), molecular biology of positive strand RNA viruses. Academic Press, London, United Kingdom.
    • (1987) Molecular Biology of Positive Strand RNA Viruses , pp. 129-152
    • King, A.M.Q.1    Ortlepp, S.A.2    Newman, J.W.I.3    McCahon, D.4
  • 20
    • 2642708375 scopus 로고    scopus 로고
    • Bovine viral diarrhea virus strain Oregon: A novel mechanism for processing of NS2-3 based on point mutations
    • Kümmerer, B. M., D. Stoll, and G. Meyers. 1998. Bovine viral diarrhea virus strain Oregon: a novel mechanism for processing of NS2-3 based on point mutations. J. Virol. 72:4127-4138.
    • (1998) J. Virol. , vol.72 , pp. 4127-4138
    • Kümmerer, B.M.1    Stoll, D.2    Meyers, G.3
  • 21
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-392.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-392
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 22
    • 0026602984 scopus 로고
    • RNA recombination in animal and plant viruses
    • Lai, M. M. C. 1992. RNA recombination in animal and plant viruses. Microbiol. Rev. 56:61-79.
    • (1992) Microbiol. Rev. , vol.56 , pp. 61-79
    • Lai, M.M.C.1
  • 23
    • 0028289946 scopus 로고
    • Molecular characterization of light chain 3
    • Mann, S. S., and J. A. Hammerback. 1994. Molecular characterization of light chain 3. J. Biol. Chem. 269:11492-11497.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11492-11497
    • Mann, S.S.1    Hammerback, J.A.2
  • 24
    • 0022425796 scopus 로고
    • Isolation of cytopathic and noncytopathic bovine viral diarrhea virus from the spleen of cattle acutely and chronically affected with bovine viral diarrhea
    • McClurkin, A. W., S. R. Bolin, and M. F. Coria. 1985. Isolation of cytopathic and noncytopathic bovine viral diarrhea virus from the spleen of cattle acutely and chronically affected with bovine viral diarrhea. J. Am. Vet. Med. Assoc. 186:568-569.
    • (1985) J. Am. Vet. Med. Assoc. , vol.186 , pp. 568-569
    • McClurkin, A.W.1    Bolin, S.R.2    Coria, M.F.3
  • 25
    • 0014300754 scopus 로고
    • Complications in cattle following vaccination with a combined bovine viral diarrhea-infectious bovine rhinotracheitis vaccine
    • McKercher, D. G., J. K. Saito, G. L. Crenshaw, and R. B. Bushnell. 1968. Complications in cattle following vaccination with a combined bovine viral diarrhea-infectious bovine rhinotracheitis vaccine. J. Am. Vet. Med. Assoc. 152:1621-1624.
    • (1968) J. Am. Vet. Med. Assoc. , vol.152 , pp. 1621-1624
    • McKercher, D.G.1    Saito, J.K.2    Crenshaw, G.L.3    Bushnell, R.B.4
  • 27
    • 0002449087 scopus 로고
    • Insertion of ubiquitin-coding sequence identified in the RNA genome of a togavirus
    • M. A. Brinton, and F. X. Heinz (ed.). American Society for Microbiology, Washington, D.C.
    • Meyers, G., T. Rümenapf, and H.-J. Thiel. 1990. Insertion of ubiquitin-coding sequence identified in the RNA genome of a togavirus, p. 25-30. In M. A. Brinton, and F. X. Heinz (ed.), New aspects of positive-strand RNA viruses. American Society for Microbiology, Washington, D.C.
    • (1990) New Aspects of Positive-strand RNA Viruses , pp. 25-30
    • Meyers, G.1    Rümenapf, T.2    Thiel, H.-J.3
  • 28
    • 0029861559 scopus 로고    scopus 로고
    • Recovery of cytopathogenic and noncytopathogenic bovine viral diarrhea viruses from cDNA constructs
    • Meyers, G., N. Tautz, P. Becher, H.-J. Thiel, and B. M. Kümmerer. 1996 Recovery of cytopathogenic and noncytopathogenic bovine viral diarrhea viruses from cDNA constructs. J. Virol. 70:8606-8613.
    • (1996) J. Virol. , vol.70 , pp. 8606-8613
    • Meyers, G.1    Tautz, N.2    Becher, P.3    Thiel, H.-J.4    Kümmerer, B.M.5
  • 29
    • 0025963978 scopus 로고
    • Viral cytopathogenicity correlated with integration of ubiquitin-coding sequences
    • 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.
    • (1991) Virology , vol.180 , pp. 602-616
    • Meyers, G.1    Tautz, N.2    Dubovi, E.J.3    Thiel, H.-J.4
  • 31
    • 0030333528 scopus 로고    scopus 로고
    • Molecular characterization of pestiviruses
    • Meyers, G., and H.-J. Thiel. 1996. Molecular characterization of pestiviruses. Adv. Virus Res. 47:53-117.
    • (1996) Adv. Virus Res. , vol.47 , pp. 53-117
    • Meyers, G.1    Thiel, H.-J.2
  • 32
    • 0030030478 scopus 로고    scopus 로고
    • Classical swine fever virus: Recovery of infectious viruses from cDNA constructs and generation of recombinant cytopathogenic defective interfering particles
    • 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.
    • (1996) J. Virol. , vol.70 , pp. 1588-1595
    • Meyers, G.1    Thiel, H.-J.2    Rümenapf, T.3
  • 33
    • 0023114840 scopus 로고
    • Variation in the intracellular polypeptide profiles from different isolates of bovine viral diarrhea virus
    • 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.
    • (1987) Arch. Virol. , vol.94 , pp. 43-53
    • Pocock, D.H.1    Howard, C.J.2    Clarke, M.C.3    Brownlie, J.4
  • 34
    • 0026718388 scopus 로고
    • Analysis of the bovine viral diarrhea virus genome for possible insertions
    • Qi, F., J. F. Ridpath, T. Lewis, S. R. Bolin, and E. S. Berry. 1992. Analysis of the bovine viral diarrhea virus genome for possible insertions. Virology 189:285-292.
    • (1992) Virology , vol.189 , pp. 285-292
    • Qi, F.1    Ridpath, J.F.2    Lewis, T.3    Bolin, S.R.4    Berry, E.S.5
  • 35
    • 0001424128 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven, Philadelphia, Pa.
    • 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. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology , pp. 931-959
    • Rice, C.M.1
  • 36
    • 0027238125 scopus 로고
    • Processing of the envelope glycoproteins of pestiviruses
    • Rümenapf, T., G. Unger, J. H. Strauss, and H.-J. Thiel. 1993. Processing of the envelope glycoproteins of pestiviruses. J. Virol. 67:3288-3294.
    • (1993) J. Virol. , vol.67 , pp. 3288-3294
    • Rümenapf, T.1    Unger, G.2    Strauss, J.H.3    Thiel, H.-J.4
  • 39
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-poly-acrylamide gel electrophoresis for the separation of proteins in the range from 1-100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-poly-acrylamide gel electrophoresis for the separation of proteins in the range from 1-100 kDa. Anal. Biochem. 146:368-379.
    • (1987) Anal. Biochem. , vol.146 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 40
    • 0027424003 scopus 로고
    • Processing of pestivirus polyprotein: Cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus
    • 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.
    • (1993) J. Virol. , vol.67 , pp. 7088-7095
    • Stark, R.1    Meyers, G.2    Rümenapf, T.3    Thiel, H.-J.4
  • 41
    • 0030960350 scopus 로고    scopus 로고
    • Serine protease of pestiviruses: Determination of cleavage sites
    • Tautz, N., K. Elbers, D. Stoll, G. Meyers, and H.-J. Thiel. 1997. Serine protease of pestiviruses: determination of cleavage sites. J. Virol. 71:5415-5422.
    • (1997) J. Virol. , vol.71 , pp. 5415-5422
    • Tautz, N.1    Elbers, K.2    Stoll, D.3    Meyers, G.4    Thiel, H.-J.5
  • 42
    • 0029798235 scopus 로고    scopus 로고
    • Cytopathogenicity of a pestivirus correlates with a 27-nucleotide insertion
    • Tautz, N., G. Meyers, R. Stark, E. J. Dubovi, and H.-J. Thiel. 1996. Cytopathogenicity of a pestivirus correlates with a 27-nucleotide insertion. J. Virol. 70:7851-7858.
    • (1996) J. Virol. , vol.70 , pp. 7851-7858
    • Tautz, N.1    Meyers, G.2    Stark, R.3    Dubovi, E.J.4    Thiel, H.-J.5
  • 43
    • 0027360808 scopus 로고
    • Processing of poly-ubiquitin in the polyprotein of an RNA virus
    • Tautz, N., G. Meyers, and H.-J. Thiel. 1993. Processing of poly-ubiquitin in the polyprotein of an RNA virus. Virology 197:74-85.
    • (1993) Virology , vol.197 , pp. 74-85
    • Tautz, N.1    Meyers, G.2    Thiel, H.-J.3
  • 44
    • 0028334978 scopus 로고
    • Pathogenesis of mucosal disease: A cytopathogenic pestivirus generated by an internal deletion
    • Tautz, N., H.-J. Thiel, E. Dubovi, and G. Meyers. 1994. Pathogenesis of mucosal disease: a cytopathogenic pestivirus generated by an internal deletion. J. Virol. 68:3289-3297.
    • (1994) J. Virol. , vol.68 , pp. 3289-3297
    • Tautz, N.1    Thiel, H.-J.2    Dubovi, E.3    Meyers, G.4
  • 45
    • 0000604899 scopus 로고    scopus 로고
    • The pestiviruses
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven, Philadelphia, Pa.
    • Thiel, H.-J., G. W. Plagemann, and V. Moennig. 1996. The pestiviruses, p. 1059-1073. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology , pp. 1059-1073
    • Thiel, H.-J.1    Plagemann, G.W.2    Moennig, V.3
  • 46
    • 0025955758 scopus 로고
    • Hog cholera virus: Molecular composition of virions from a pestivirus
    • 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.
    • (1991) J. Virol. , vol.65 , pp. 4705-4712
    • Thiel, H.-J.1    Stark, R.2    Weiland, E.3    Rümenapf, T.4    Meyers, G.5
  • 48
    • 0028872259 scopus 로고
    • Pestivirus NS3 (p80) protein possesses RNA helicase activity
    • Warrener, P., and M. S. Collett. 1995. Pestivirus NS3 (p80) protein possesses RNA helicase activity. J. Virol. 69:1720-1726.
    • (1995) J. Virol. , vol.69 , pp. 1720-1726
    • Warrener, P.1    Collett, M.S.2
  • 49
    • 0025785808 scopus 로고
    • Pestivirus gene expression: Protein p80 of bovine viral diarrhea virus is a proteinase involved in polyprotein processing
    • Wiskerchen, M., 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.
    • (1991) Virology , vol.184 , pp. 341-350
    • Wiskerchen, M.1    Collett, M.S.2
  • 50
    • 0031010133 scopus 로고    scopus 로고
    • Bovine viral diarrhea virus NS3 serine proteinase: Polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication
    • Xu, J., E. Mendez, P. R. Caron, C. Lin, M. A. Murcko, M. S. Collett, and C. M. Rice. 1997. Bovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication. J. Virol. 71:5312-5322.
    • (1997) J. Virol. , vol.71 , pp. 5312-5322
    • Xu, J.1    Mendez, E.2    Caron, P.R.3    Lin, C.4    Murcko, M.A.5    Collett, M.S.6    Rice, C.M.7


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