Summary
Bovine Viral Diarrhea Virus (BVDV) polypeptides present in infected cells are the result of the processing of the polyprotein translated from the large single open reading frame of the BVDV genomic RNA. The presence of these proteins in infected cells was studied by radiolabeling under hypertonic conditions and with the aid of radioimmunoprecipitation. The genomic mapping of these polypeptides suggests a complex pattern of processing which involves cellular and viral proteases. The consistent absence of 80k in noncytopathic isolates of BVDV suggests that the processing of the viral polyprotein is different in cytopathic and noncytopathic biotypes of BVDV. The antigenic structure of BVDV was studied with a panel of monoclonal antibodies (MABs) prepared against the Singer isolate of BVDV. Neutralizing MABs were found to bind the 56–58k polypeptide, providing evidence that this glycoprotein is present on the surface of the virion and carries neutralization epitopes. Antigenic analyses with the panel of MABs reveals extensive antigenic heterogeneity among BVDV field isolates. MABs were used to determine the frequency of neutralization escape mutants in stocks of BVDV. Plaque-purified BVDV stocks contain neutralization escape mutants with a frequency of 10-2.47
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Almond JW, Stanway G, Cann AJ, Westrop GD, Evans DM, Ferguson M, Minor PD, Schild GC (1984) New poliovirus vaccines: a molecular approach. Vaccine 2: 177–82
Baker JC (1987) Bovine viral diarrhea virus: a review. J Am Vet Med Assoc 190: 1449–58
Birrer MJ, Udem S, Nathenson S, Bloom BR (1981) Antigenic variants of measles virus. Nature 293: 67
Bolin SR, McClurkin AW, Cuthp RC, Coria MF (1985) Severe cHnical disease induced in cattle persistently infected with noncytopathic bovine viral diarrhea virus by superinfection with cytopathic bovine viral diarrhea virus. Am J Vet Res 46: 573–576
Bolwell C, Parry NR, Rowlands DJ, Brown F, Ouldridge EJ (1986) Foot and mouth disease virus variants with broad and narrow antigenic spectra. In: Lerner RA, Channock RN, Brown F (eds). Vaccines 86. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, p 51
Brownlie J, Clarke MC, Howard CJ (1984) Experimental production of fatal mucosal disease in cattle. Vet Ree 114: 535–537
Collett MS, Anderson DK, Retzel E (1988) Comparisons of the pestivirus bovine viral diarrhoea virus with members of the flaviviridae. J Gen Virol 69: 2637–43
Collett MS, Larson R, Beizer SK, Retzel E (1988) Proteins encoded by bovine viral diarrhea virus: the genomic organization of a pestivirus. Virology 165: 200–208
Collett MS, Larson R, Gold C, Strick D, Anderson DK, Purchio AF (1988) Molecular cloning and nucleotide sequence of the pestivirus Bovine Viral Diarrhea virus. Virology 165: 191–199
Commerce Dpt, Bureau of the Census (1984) 1982 Census of Agriculture. US Government Publications
Corapi WV, Donis RO, Dubovi EJ (1988) Monoclonal antibody analyses of cytopathic and noncytopathic viruses from fatal bovine viral diarrhea virus infections. J Virol 62: 2823–2827
Crainic R, Couillin P, Blondel B, Cabau N, Bouse A, Horodniceau F (1983) Natural variation of pohovirus epitopes. Infect Immun 41: 1217–23
Diamond DC, Jameson BA, Bonin J, Kohara M, Abe S, Crainic R, Wimmer E (1985) Antigenic variation and resistance to neutralization in polio virus type 1. Science 229: 1090–93
Done JT, Terlecki S, Richardson C, Harkness JW, Sands JJ, Patterson DSP, Sweasey D, Shaw IG (1980) Bovine virus diarrhea-mucosal disease virus: pathogenicity for the fetal calf following maternal infection. Vet Ree 108: 473–479
Donis RO, Bean WJ, Webster RG (1989) Distinct hneages of influenza virus H4 hemagglutinin genes in different regions of the world. Virology 169: 408–417
Donis RO, Corapi WV, Dubovi EJ (1988) Neutralizing monoclonal antibodies to BVD virus bind to the 56–58k polypeptide. J Gen Virol 69: 77–86
Donis RO, Dubovi EJ (1987) Glycoproteins of bovine viral diarrhea-mucosal disease virus in infected bovine cells. J Gen Virol 68: 1607–1616
Donis RO, Dubovi EJ (1987) Differences in virus-induced polypeptides in cells infected by cytopathic and noncytopathic biotypes of bovine virus diarrhea-mucosal disease virus. Virology 58: 168–173
Donis RO, Dubovi J (1987) Characterization of bovine viral diarrhea-mucosal disease virus-specific proteins in bovine cells. J Gen Virol 68: 1597–1605
Dubovi EJ, White T, Cordell B, Dales B, Donis RO (1987) Expression of a glycoprotein antigen of bovine viral diarrhea virus that eHcits neutralizing antibodies in mice. In: Chanock M, Lerner R (eds) Modern approaches to new vaccines. Cold Spring Harbor Laboratory, New York, pp 435–439
Eigen M (1971) Self-organization of matter and the evolution of biological macro- molecules. Naturwissenschaften 58: 465–482
Eigen M, Schuster P (1979) The hypercycle: a principle of natural self-organization. Springer, Berhn Heidelberg New York Tokyo
Emini EA, Jameson BA, Lewis AJ, Larsen GR, Wimmer E (1982) Pohovirus neutralization epitopes: analysis and localization with neutralizing monoclonal antibodies. J Virol 43: 997–1002
Gillespie JH, Coggins L, Thompson J, Baker JA (1961) Comparison by neutralization tests of strains of virus isolated from virus diarrhea and mucosal disease. Cornell Vet 51: 155–159
Gillespie JH, Madin SH, Darby NB (1962) Cellular resistance in tissue culture, induced by noncytopathogenic strains, to a cytopathogenic strain of virus diarrhea virus of cattle. Proc Soc Exp Biol Med 110: 248–250
Goudswaard J, Van Der Donk JA, Noordzij A (1978) Protein A reactivity of various mammalian immunoglobulins. Scand J Immunol 8: 21–28
Harkness JW (1987) The control of bovine viral diarrhoea virus infection. Ann Rech Vet 18: 167–74
Harkness JW, Roeder PL, Drew T, Wood L, Jeffrey M (1985) The efficacy of an experimental inactivated BVD-MD vaccine. CEC seminar: Pestivirus infection of ruminants
Kessler SW (1975) Rapid isolation of antigens from cells with a staphylococcal protein A-antibody adsorbent: parameters of the interaction of antibody-antigen complexes with protein A. J Immunol 115: 1617–1624
Kniazeff AJ, Huck RA, Jarrett WFH, Prichard WR, Ramsey FK, Schipper IA, Stober M, Liess B (1961) Antigenic relationship of some isolates of bovine viral diarrhea-mucosal disease viruses from the United States, Great Britain and West Germany. Vet Ree 73: 768–769
Kniazeff AJ, Pritchard WR (1960) Antigenic relationships in the bovine viral diarrhea- mucosal disease complex. Proceedings U.S.A.H.A. 64: 345–350
Lee KM, Gillespie JH (1957) Propagation of virus diarrhea virus of cattle in tissue cuhure. Am J Vet Res 18: 952–953
Lobmann M, Charher P, Florent G, Zygraich N (1984) Clinical evaluation of a temperature sensitive bovine viral diarrhea vaccine strain. Am J Vet Res 45: 2498–2504
Nuss DL, Oppermann H, Koch G (1975) Selective inhibition of host protein synthesis in RNA-virus-infected cells. Proc Nat Acad Sci 72: 1258–1262
Office for Statistics, European Community ( 1989 ) Agricultural Statistical Yearbook 1989. Brussels-Luxembourg CECA-CEE-CEEA
Palese P, Young JF (1982) Variation of influenza A, B, and C viruses. Science 215: 1468–74
Peters AR (1987) Vaccines for respiratory disease in cattle. Vaccine 5: 164–69
Portner A, Webster RG, Bean WJ (1980) Similar frequencies of antigenic variants in Sendai, vesicular stomatitis and influenza A viruses. Virology 104: 235–41
Prabhakar BS, Haspel MD, McChntock PR, Notkins AL (1982) High frequency of antigenic variants among naturally occurring human Coxsackie B4 virus isolates identified by monoclonal antibodies. Nature 300: 374–77
Prabhakar BS, Menegus MA, Notkins AL (1985) Detection of conserved and non- conserved epitopes on Coxsackie virus B4: frequency of antigenic change. Virology 146: 302–7
Sheshberadaran H, Norrby E (1986) Characterization of epitopes on the measles virus hemagglutinin. Virology 152: 58–67
Svitkin YV, Lyapustin VN, Lashkevich VA, Agol VI (1984) Differences between translation products of tick-borne encephalitis virus RNA in cell-free systems from Krebs-2 cells and rabbit reticulocytes: involvement of membranes in the processing of nascen precursors of flavivirus structural proteins. Virology 135: 536–41
Underdahl NR, Grace OD, Hoerlein AB (1957) Cultivation in tissue culture of cytopathogenic agent from bovine mucosal disease. Proc Soc Exp Biol Med 94: 795–797
Vonderfecht HE (1980) Why I recommend vaccinating cattle against bovine virus diarrhea (BVD). VMS AC Vet Med Small Anim CHn 75: 853–858
Webster RG, Laver WG, Air GM, Schild GC (1982) Molecular mechanisms of variation in influenza viruses. Nature 296: 115–21
Wellink J, Van-Kammen A (1988) Proteases involved in the processing of viral polyproteins. Brief review. Arch Virol 98: 1–26
Wiktor TJ, Koprowski H (1980) Antigenic variants of rabies virus. J Exp Med 152: 99–16
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1991 Springer-Verlag
About this paper
Cite this paper
Donis, R.O., Corapi, W.V., Dubovi, E.J. (1991). Bovine viral diarrhea virus proteins and their antigenic analyses. In: Liess, B., Moennig, V., Pohlenz, J., Trautwein, G. (eds) Ruminant Pestivirus Infections. Archives of Virology, vol 3. Springer, Vienna. https://doi.org/10.1007/978-3-7091-9153-8_4
Download citation
DOI: https://doi.org/10.1007/978-3-7091-9153-8_4
Publisher Name: Springer, Vienna
Print ISBN: 978-3-211-82279-1
Online ISBN: 978-3-7091-9153-8
eBook Packages: Springer Book Archive