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VP2 is the major exposed protein on orbiviruses

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Summary

Iodination of African horsesickness virus and epizootic hemorrhagic disease virus resulted in labeling of VP2 and not of the other capsid protein, VP5, suggesting that VP2 is the major surface exposed protein of these orbiviruses.

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References

  1. Bremer CW (1976) A gel electrophoretic study of the protein and nucleic acid components of African horsesickness virus. Onderstepoort J Vet Res 23: 193–199

    Google Scholar 

  2. Eaton BT, Gould AR, Hyatt AD, Coupar BEH, Martyn JC, White JR (1991) A bluetongue serogroup-reactive epitope in the amino terminal half of the major core protein VP7 is accessible on the surface of bluetongue virus particles. Virology 180: 687–696

    Google Scholar 

  3. Gould AR, Hyatt AD, Eaton BT (1988) Morphogenesis of a bluetongue virus variant with an amino acid alteration at a neutralization site in the outer coat protein, VP2. Virology 165: 23–32

    Google Scholar 

  4. Grieder FB, Schultz KT (1989) Conformationally dependent epitopes of bluetongue virus neutralizing antigen. Viral Immunol 2: 17–24

    Google Scholar 

  5. Huismans H, Bremer CW, Barber TL (1979) The nucleic acid and proteins of epizootic hemorrhagic disease virus. Onderstepoort J Vet Res 46: 95–104

    Google Scholar 

  6. Huismans H, Van Der Walt NT, Cloete M, Erasmus BJ (1987) Isolation of a capsid protein of bluetongue virus that induces a protective immune response in sheep. Virology 157: 172–179

    Google Scholar 

  7. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227: 680–685

    Google Scholar 

  8. Lee B, Richards FM (1971) The interpretation of protein structures: estimation of static accessibility. J Mol Biol 55: 379–400

    Google Scholar 

  9. Lewis SA, Grubman MJ (1990) Bluetongue virus: surface exposure of VP7. Virus Res 16: 17–26

    Google Scholar 

  10. Martin SA, Pett DM, Zweerink HJ (1973) Studies on the topography of reovirus and bluetongue virus capsid proteins. J Virol 12: 194–198

    Google Scholar 

  11. Mecham JO, Dean VC, Jochim MM (1986) Correlation of serotype specificity and protein structure of the five U.S. serotypes of bluetongue virus. J Gen Virol 67: 2617–2624

    Google Scholar 

  12. Mecham JO, Jochim MM (1990) Monoclonal antibodies to bluetongue virus define two neutralizing epitopes and a haemagglutinating epitope. Viral Immunol 3: 161–170

    Google Scholar 

  13. Reay P (1982) Use of N-bromosuccinimide for the iodination of proteins for radioimmunoassay. Ann Clin Biochem 19: 129–133

    Google Scholar 

  14. Spence RP, Moore NF, Nuttall PA (1984) The biochemistry of orbiviruses (brief review). Arch Virol 82: 1–18

    Google Scholar 

  15. Sundin DR, Dean VC, DuBard KM, Mecham JO (1989) In vitro neutralization of antigenic variants of bluetongue virus is related to in vivo protection. Viral Immunol 2: 195–203

    Google Scholar 

  16. Thompson JA, Lau AL, Cunningham DD (1987) Selective radiolabeling of cell surface proteins to a high specific activity. Biochemistry 26: 743–750

    Google Scholar 

  17. Van Dijk AA, Huismans H (1980) The in vitro activation and further characterization of the bluetongue virus-associated transcriptase. Virology 104: 347–356

    Google Scholar 

  18. Wray W, Boulikas T, Wray VP, Hancock R (1981) Silver staining of proteins in polyacrylamide gels. Anal Biochem 118: 197–203

    Google Scholar 

  19. Yamasaki RB, Vega A, Feeney RE (1980) Modification of available arginine residues in proteins by p-hydroxyphenylglyoxal. Anal Biochem 109: 32–40

    Google Scholar 

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Authors and Affiliations

  1. Agricultural Research Service, North Atlantic Area U.S. Department of Agriculture, Plum Island Animal Disease Center, Greenport, New York, U.S.A.

    S. A. Lewis & M. J. Grubman

Authors
  1. S. A. Lewis
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  2. M. J. Grubman
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Lewis, S.A., Grubman, M.J. VP2 is the major exposed protein on orbiviruses. Archives of Virology 121, 233–236 (1991). https://doi.org/10.1007/BF01316758

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  • DOI: https://doi.org/10.1007/BF01316758

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