Abstract
To study which proteins of classical swine fever virus (CSFV) are able to confer protective immunity in swine, N-terminal autoprotease, viral core protein, and the three structural glycoproteins were expressed via vaccinia virus recombinants (VVR). CSFV proteins synthesized in cells infected with VVR showed migration characteristics on sodium dodecyl sulfate gels identical to those of their respective CSFV counterparts. Apparently authentic dimerization of the recombinant glycoproteins was observed. The glycoproteins E0 and E2 were detected on the surfaces of VVR-infected cells. In protection experiments, swine were immunized with the different VVR, and the generation of humoral immune response was monitored. Only animals vaccinated with VVR expressing E0 and/or E2 resisted a lethal challenge infection with CSFV. Glycoprotein E0 represents a second determinant for the induction of protective immunity against classical swine fever.
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- Byrne J. A., Oldstone M. B. Biology of cloned cytotoxic T lymphocytes specific for lymphocytic choriomeningitis virus: clearance of virus in vivo. J Virol. 1984 Sep;51(3):682–686. doi: 10.1128/jvi.51.3.682-686.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Collett M. S., Larson R., Belzer S. K., Retzel E. Proteins encoded by bovine viral diarrhea virus: the genomic organization of a pestivirus. Virology. 1988 Jul;165(1):200–208. doi: 10.1016/0042-6822(88)90673-3. [DOI] [PubMed] [Google Scholar]
- Cranage M. P., Kouzarides T., Bankier A. T., Satchwell S., Weston K., Tomlinson P., Barrell B., Hart H., Bell S. E., Minson A. C. Identification of the human cytomegalovirus glycoprotein B gene and induction of neutralizing antibodies via its expression in recombinant vaccinia virus. EMBO J. 1986 Nov;5(11):3057–3063. doi: 10.1002/j.1460-2075.1986.tb04606.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Greiser-Wilke I., Dittmar K. E., Liess B., Moennig V. Immunofluorescence studies of biotype-specific expression of bovine viral diarrhoea virus epitopes in infected cells. J Gen Virol. 1991 Aug;72(Pt 8):2015–2019. doi: 10.1099/0022-1317-72-8-2015. [DOI] [PubMed] [Google Scholar]
- Hulst M. M., Himes G., Newbigin E., Moormann R. J. Glycoprotein E2 of classical swine fever virus: expression in insect cells and identification as a ribonuclease. Virology. 1994 May 1;200(2):558–565. doi: 10.1006/viro.1994.1218. [DOI] [PubMed] [Google Scholar]
- Hulst M. M., Westra D. F., Wensvoort G., Moormann R. J. Glycoprotein E1 of hog cholera virus expressed in insect cells protects swine from hog cholera. J Virol. 1993 Sep;67(9):5435–5442. doi: 10.1128/jvi.67.9.5435-5442.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kimman T. G., Bianchi A. T., Wensvoort G., de Bruin T. G., Meliefste C. Cellular immune response to hog cholera virus (HCV): T cells of immune pigs proliferate in vitro upon stimulation with live HCV, but the E1 envelope glycoprotein is not a major T-cell antigen. J Virol. 1993 May;67(5):2922–2927. doi: 10.1128/jvi.67.5.2922-2927.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kozak M. The scanning model for translation: an update. J Cell Biol. 1989 Feb;108(2):229–241. doi: 10.1083/jcb.108.2.229. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Meyers G., Rümenapf T., Thiel H. J. Molecular cloning and nucleotide sequence of the genome of hog cholera virus. Virology. 1989 Aug;171(2):555–567. doi: 10.1016/0042-6822(89)90625-9. [DOI] [PubMed] [Google Scholar]
- Moennig V., Plagemann P. G. The pestiviruses. Adv Virus Res. 1992;41:53–98. doi: 10.1016/s0065-3527(08)60035-4. [DOI] [PubMed] [Google Scholar]
- Moss B. Vaccinia virus: a tool for research and vaccine development. Science. 1991 Jun 21;252(5013):1662–1667. doi: 10.1126/science.2047875. [DOI] [PubMed] [Google Scholar]
- Rümenapf T., Meyers G., Stark R., Thiel H. J. Hog cholera virus--characterization of specific antiserum and identification of cDNA clones. Virology. 1989 Jul;171(1):18–27. doi: 10.1016/0042-6822(89)90506-0. [DOI] [PubMed] [Google Scholar]
- Rümenapf T., Stark R., Meyers G., Thiel H. J. Structural proteins of hog cholera virus expressed by vaccinia virus: further characterization and induction of protective immunity. J Virol. 1991 Feb;65(2):589–597. doi: 10.1128/jvi.65.2.589-597.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rümenapf T., Unger G., Strauss J. H., Thiel H. J. Processing of the envelope glycoproteins of pestiviruses. J Virol. 1993 Jun;67(6):3288–3294. doi: 10.1128/jvi.67.6.3288-3294.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schneider R., Unger G., Stark R., Schneider-Scherzer E., Thiel H. J. Identification of a structural glycoprotein of an RNA virus as a ribonuclease. Science. 1993 Aug 27;261(5125):1169–1171. doi: 10.1126/science.8356450. [DOI] [PubMed] [Google Scholar]
- Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem. 1987 Nov 1;166(2):368–379. doi: 10.1016/0003-2697(87)90587-2. [DOI] [PubMed] [Google Scholar]
- Stark R., Rümenapf T., Meyers G., Thiel H. J. Genomic localization of hog cholera virus glycoproteins. Virology. 1990 Jan;174(1):286–289. doi: 10.1016/0042-6822(90)90076-4. [DOI] [PubMed] [Google Scholar]
- Susa M., König M., Saalmüller A., Reddehase M. J., Thiel H. J. Pathogenesis of classical swine fever: B-lymphocyte deficiency caused by hog cholera virus. J Virol. 1992 Feb;66(2):1171–1175. doi: 10.1128/jvi.66.2.1171-1175.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Terpstra C., Wensvoort G. The protective value of vaccine-induced neutralising antibody titres in swine fever. Vet Microbiol. 1988 Feb;16(2):123–128. doi: 10.1016/0378-1135(88)90036-3. [DOI] [PubMed] [Google Scholar]
- Thiel H. J., Stark R., Weiland E., Rümenapf T., Meyers G. Hog cholera virus: molecular composition of virions from a pestivirus. J Virol. 1991 Sep;65(9):4705–4712. doi: 10.1128/jvi.65.9.4705-4712.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Walter P., Lingappa V. R. Mechanism of protein translocation across the endoplasmic reticulum membrane. Annu Rev Cell Biol. 1986;2:499–516. doi: 10.1146/annurev.cb.02.110186.002435. [DOI] [PubMed] [Google Scholar]
- Weiland E., Ahl R., Stark R., Weiland F., Thiel H. J. A second envelope glycoprotein mediates neutralization of a pestivirus, hog cholera virus. J Virol. 1992 Jun;66(6):3677–3682. doi: 10.1128/jvi.66.6.3677-3682.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weiland E., Stark R., Haas B., Rümenapf T., Meyers G., Thiel H. J. Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer. J Virol. 1990 Aug;64(8):3563–3569. doi: 10.1128/jvi.64.8.3563-3569.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wensvoort G., Boonstra J., Bodzinga B. G. Immunoaffinity purification and characterization of the envelope protein E1 of hog cholera virus. J Gen Virol. 1990 Mar;71(Pt 3):531–540. doi: 10.1099/0022-1317-71-3-531. [DOI] [PubMed] [Google Scholar]
- Yap K. L., Ada G. L., McKenzie I. F. Transfer of specific cytotoxic T lymphocytes protects mice inoculated with influenza virus. Nature. 1978 May 18;273(5659):238–239. doi: 10.1038/273238a0. [DOI] [PubMed] [Google Scholar]
- van Rijn P. A., Miedema G. K., Wensvoort G., van Gennip H. G., Moormann R. J. Antigenic structure of envelope glycoprotein E1 of hog cholera virus. J Virol. 1994 Jun;68(6):3934–3942. doi: 10.1128/jvi.68.6.3934-3942.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- van Zijl M., Wensvoort G., de Kluyver E., Hulst M., van der Gulden H., Gielkens A., Berns A., Moormann R. Live attenuated pseudorabies virus expressing envelope glycoprotein E1 of hog cholera virus protects swine against both pseudorabies and hog cholera. J Virol. 1991 May;65(5):2761–2765. doi: 10.1128/jvi.65.5.2761-2765.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]