Skip to main content
Journal of Virology logoLink to Journal of Virology
. 1991 Feb;65(2):589–597. doi: 10.1128/jvi.65.2.589-597.1991

Structural proteins of hog cholera virus expressed by vaccinia virus: further characterization and induction of protective immunity.

T Rümenapf 1, R Stark 1, G Meyers 1, H J Thiel 1
PMCID: PMC239796  PMID: 1987372

Abstract

A cDNA fragment covering the genomic region that encodes the structural proteins of hog cholera virus (HCV) was inserted into the tk gene of vaccinia virus. Expression studies with vaccinia virus/HCV recombinants led to identification of HCV-specific proteins. The putative HCV core protein p23 was demonstrated for the first time by using an antiserum against a bacterial fusion protein. The glycoproteins expressed by vaccinia virus/HCV recombinant migrated on sodium dodecyl sulfate-gels identically to glycoproteins precipitated from HCV-infected cells. A disulfide-linked heterodimer between gp55 and gp33 previously detected in HCV-infected cells was also demonstrated after infection with the recombinant virus. The vaccinia virus system allowed us to identify, in addition to the heterodimer, a disulfide-linked homodimer of HCV gp55. The vaccinia virus/HCV recombinant that expressed all four structural proteins induced virus-neutralizing antibodies in mice and swine. After immunization of pigs with this recombinant virus, full protection against a lethal challenge with HCV was achieved. A construct that lacked most of the HCV gp55 gene failed to induce neutralizing antibodies but induced protective immunity.

Full text

PDF
589

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bolin S., Moennig V., Kelso Gourley N. E., Ridpath J. Monoclonal antibodies with neutralizing activity segregate isolates of bovine viral diarrhea virus into groups. Brief report. Arch Virol. 1988;99(1-2):117–123. doi: 10.1007/BF01311029. [DOI] [PubMed] [Google Scholar]
  2. Brown F. How do vaccinia-vectored vaccines fit into animal immunization programmes? Res Virol. 1989 Sep-Oct;140(5):474–476. doi: 10.1016/s0923-2516(89)80129-3. [DOI] [PubMed] [Google Scholar]
  3. Colett M. S., Larson R., Gold C., Strick D., Anderson D. K., Purchio A. F. Molecular cloning and nucleotide sequence of the pestivirus bovine viral diarrhea virus. Virology. 1988 Jul;165(1):191–199. doi: 10.1016/0042-6822(88)90672-1. [DOI] [PubMed] [Google Scholar]
  4. Collett M. S., Anderson D. K., Retzel E. Comparisons of the pestivirus bovine viral diarrhoea virus with members of the flaviviridae. J Gen Virol. 1988 Oct;69(Pt 10):2637–2643. doi: 10.1099/0022-1317-69-10-2637. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. Collett M. S., Moennig V., Horzinek M. C. Recent advances in pestivirus research. J Gen Virol. 1989 Feb;70(Pt 2):253–266. doi: 10.1099/0022-1317-70-2-253. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Deinhardt F., Bergholz C., Hunsmann G., Schneider J., Thiel H. J., Beug H., Schäfer W. Studies of simian sarcoma and simian sarcoma-associated virus. I. Analysis of viral structural proteins, and preparation and characterization of antiserum specific for viral envelope components. Z Naturforsch C. 1978 Nov-Dec;33(11-12):969–980. doi: 10.1515/znc-1978-11-1227. [DOI] [PubMed] [Google Scholar]
  9. Donis R. O., Corapi W., Dubovi E. J. Neutralizing monoclonal antibodies to bovine viral diarrhoea virus bind to the 56K to 58K glycoprotein. J Gen Virol. 1988 Jan;69(Pt 1):77–86. doi: 10.1099/0022-1317-69-1-77. [DOI] [PubMed] [Google Scholar]
  10. Drillien R., Spehner D. Physical mapping of vaccinia virus temperature-sensitive mutations. Virology. 1983 Dec;131(2):385–393. doi: 10.1016/0042-6822(83)90506-8. [DOI] [PubMed] [Google Scholar]
  11. Goding J. W., Harris A. W. Subunit structure of cell surface proteins: disulfide bonding in antigen receptors, Ly-2/3 antigens, and transferrin receptors of murine T and B lymphocytes. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4530–4534. doi: 10.1073/pnas.78.7.4530. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Henikoff S. Unidirectional digestion with exonuclease III in DNA sequence analysis. Methods Enzymol. 1987;155:156–165. doi: 10.1016/0076-6879(87)55014-5. [DOI] [PubMed] [Google Scholar]
  13. Jonjić S., del Val M., Keil G. M., Reddehase M. J., Koszinowski U. H. A nonstructural viral protein expressed by a recombinant vaccinia virus protects against lethal cytomegalovirus infection. J Virol. 1988 May;62(5):1653–1658. doi: 10.1128/jvi.62.5.1653-1658.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kaplan C. Vaccinia virus: a suitable vehicle for recombinant vaccines? Arch Virol. 1989;106(1-2):127–139. doi: 10.1007/BF01311044. [DOI] [PubMed] [Google Scholar]
  15. Kessler S. W. Use of protein A-bearing staphylococci for the immunoprecipitation and isolation of antigens from cells. Methods Enzymol. 1981;73(Pt B):442–459. doi: 10.1016/0076-6879(81)73084-2. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  18. Mackett M., Smith G. L., Moss B. Vaccinia virus: a selectable eukaryotic cloning and expression vector. Proc Natl Acad Sci U S A. 1982 Dec;79(23):7415–7419. doi: 10.1073/pnas.79.23.7415. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Mackett M., Smith G. L. Vaccinia virus expression vectors. J Gen Virol. 1986 Oct;67(Pt 10):2067–2082. doi: 10.1099/0022-1317-67-10-2067. [DOI] [PubMed] [Google Scholar]
  20. Magar R., Minocha H. C., Lecomte J. Bovine viral diarrhea virus proteins: heterogeneity of cytopathogenic and non-cytopathogenic strains and evidence of a 53K glycoprotein neutralization epitope. Vet Microbiol. 1988 Apr;16(4):303–314. doi: 10.1016/0378-1135(88)90012-0. [DOI] [PubMed] [Google Scholar]
  21. Melancon P., Garoff H. Processing of the Semliki Forest virus structural polyprotein: role of the capsid protease. J Virol. 1987 May;61(5):1301–1309. doi: 10.1128/jvi.61.5.1301-1309.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. 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]
  23. Moormann R. J., Warmerdam P. A., van der Meer B., Schaaper W. M., Wensvoort G., Hulst M. M. Molecular cloning and nucleotide sequence of hog cholera virus strain Brescia and mapping of the genomic region encoding envelope protein E1. Virology. 1990 Jul;177(1):184–198. doi: 10.1016/0042-6822(90)90472-4. [DOI] [PubMed] [Google Scholar]
  24. Osburn B. I., Clarke G. L., Stewart W. C., Sawyer M. Border disease-like syndrome in lambs: antibodies to hog cholera and bovine viral diarrhea viruses. J Am Vet Med Assoc. 1973 Nov 15;163(10):1165–1167. [PubMed] [Google Scholar]
  25. Rice C. M., Franke C. A., Strauss J. H., Hruby D. E. Expression of Sindbis virus structural proteins via recombinant vaccinia virus: synthesis, processing, and incorporation into mature Sindbis virions. J Virol. 1985 Oct;56(1):227–239. doi: 10.1128/jvi.56.1.227-239.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. 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]
  27. Schmaljohn A. L., Johnson E. D., Dalrymple J. M., Cole G. A. Non-neutralizing monoclonal antibodies can prevent lethal alphavirus encephalitis. Nature. 1982 May 6;297(5861):70–72. doi: 10.1038/297070a0. [DOI] [PubMed] [Google Scholar]
  28. 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]
  29. 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]
  30. Strandström H., Veijalainen P., Moennig V., Hunsmann G., Schwarz H., Schäfer W. C-type particles produced by a permanent cell line from a leukemic pig. I. Origin and properties of the host cells and some evidence for the occurrence of C-type-like particles. Virology. 1974 Jan;57(1):175–178. doi: 10.1016/0042-6822(74)90118-4. [DOI] [PubMed] [Google Scholar]
  31. Strebel K., Beck E., Strohmaier K., Schaller H. Characterization of foot-and-mouth disease virus gene products with antisera against bacterially synthesized fusion proteins. J Virol. 1986 Mar;57(3):983–991. doi: 10.1128/jvi.57.3.983-991.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. 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]
  33. 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]
  34. Westaway E. G., Brinton M. A., Gaidamovich SYa, Horzinek M. C., Igarashi A., Käriäinen L., Lvov D. K., Porterfield J. S., Russell P. K., Trent D. W. Togaviridae. Intervirology. 1985;24(3):125–139. doi: 10.1159/000149632. [DOI] [PubMed] [Google Scholar]
  35. Wraith D. C., Vessey A. E., Askonas B. A. Purified influenza virus nucleoprotein protects mice from lethal infection. J Gen Virol. 1987 Feb;68(Pt 2):433–440. doi: 10.1099/0022-1317-68-2-433. [DOI] [PubMed] [Google Scholar]
  36. Yilma T., Hsu D., Jones L., Owens S., Grubman M., Mebus C., Yamanaka M., Dale B. Protection of cattle against rinderpest with vaccinia virus recombinants expressing the HA or F gene. Science. 1988 Nov 18;242(4881):1058–1061. doi: 10.1126/science.3194758. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES