1887

Abstract

Twelve neutralizing monoclonal antibodies (MAbs) against the fish rhabdovirus, infectious haematopoietic necrosis virus (IHNV), were used to select 20 MAb escape mutants. The nucleotide sequence of the entire glycoprotein (G) gene was determined for six mutants representing differing cross-neutralization patterns and each had a single nucleotide change leading to a single amino acid substitution within one of three regions of the protein. These data were used to design nested PCR primers to amplify portions of the G gene of the 14 remaining mutants. When the PCR products from these mutants were sequenced, they also had single nucleotide substitutions coding for amino acid substitutions at the same, or nearby, locations. Of the 20 mutants for which all or part of the glycoprotein gene was sequenced, two MAbs selected mutants with substitutions at amino acids 230–231 (antigenic site I) and the remaining MAbs selected mutants with substitutions at amino acids 272–276 (antigenic site II). Two MAbs that selected mutants mapping to amino acids 272–276, selected other mutants that mapped to amino acids 78–81, raising the possibility that this portion of the N terminus of the protein was part of a discontinuous epitope defining antigenic site II. CLUSTAL alignment of the glycoproteins of rabies virus, vesicular stomatitis virus and IHNV revealed similarities in the location of the neutralizing epitopes and a high degree of conservation among cysteine residues, indicating that the glycoproteins of three different genera of animal rhabdoviruses may share a similar three-dimensional structure in spite of extensive sequence divergence.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-77-12-3033
1996-12-01
2024-03-28
Loading full text...

Full text loading...

/deliver/fulltext/jgv/77/12/JV0770123033.html?itemId=/content/journal/jgv/10.1099/0022-1317-77-12-3033&mimeType=html&fmt=ahah

References

  1. Air G. M., Laver W. G., Webster R. G. 1990; Mechanism of antigenic variation in an individual epitope on influenza virus N9 neuraminidase. Journal of Virology 64:5797–5803
    [Google Scholar]
  2. Benmansour A., Leblois H., Coulon P., Tuffereau C., Gaudin Y., Flamand A., Lafay F. 1991; Antigenicity of rabies virus glycoprotein. Journal of Virology 65:4198–4203
    [Google Scholar]
  3. Benmansour A., Brahimi M., Tuffereau C., Coulon P., Lafay F., Flamand A. 1992; Rapid sequence evolution of street rabies glycoprotein is related to the highly heterogeneous nature of the viral population. Virology 187:33–45
    [Google Scholar]
  4. Coulon P., Rollin P., Aubert M., Flamand A. 1982; Molecular basis of rabies virus virulence. I. Selection of avirulent mutants of the CVS strain with anti–G monoclonal antibodies. Journal of General Virology 61:97–100
    [Google Scholar]
  5. Coulon P., Rollin P. E., Flamand A. 1983; Molecular basis of rabies virus virulence. II. Identification of a site on the CVS glycoprotein associated with virulence. Journal of General Virology 64:693–696
    [Google Scholar]
  6. Dietzschold B., Wunner W. H., Wiktor T. J., Lopes A. D., Lafon M., Smith C. L., Koprowski H. 1983; Characterization of an antigenic determinant of the glycoprotein that correlates with pathogenicity of rabies virus. Proceedings of the National Academy of Sciences, USA 80:70–74
    [Google Scholar]
  7. Dietzschold B., Gore M., Marchadier D., Niu H. -S., Bunschoten H. M., Otvos L., Wunner W. H., Ertl H. C. J., Osterhaus A. D. M. E., Koprowski H. 1990; Structural and immunological characterization of a linear virus-neutralizing epitope of the rabies virus glycoprotein and its possible use in a synthetic vaccine. Journal of Virology 64:3804–3809
    [Google Scholar]
  8. Domingo E., Diez J., Martinez M. A., Hernandez J., Holguin A., Borrego B., Mateu M. G. 1993; New observations on antigenic diversification of RNA viruses. Antigenic variation is not dependent on immune selection. Journal of General Virology 74:2039–2045
    [Google Scholar]
  9. Engel king H. M., Leong J. C. 1989; The glycoprotein from infectious hematopoietic necrosis virus elicits neutralizing antibody and protective responses. Virus Research 13:213–230
    [Google Scholar]
  10. Fijan N., Sulimanovic D., Bearzotti M., Muzinic D., Zwillenberg L. O., Chilmonezyk S., Vautherot J. F., De Kinkelin P. 1983; Some properties of the Epithelioma papulosum cyprini (EPC) cell line from carp Cyprinus carpio . Annales de I’Institut Pasteur/Virologie 134E:207–220
    [Google Scholar]
  11. Gaudin Y., Ruigrok R. W. H., Tuffereau C., Knossow M., Flamand A. 1992; Rabies virus glycoprotein is a trimer. Virology 187:627–632
    [Google Scholar]
  12. Gaudin Y., Ruigrok R. W. H., Knossow M., Flamand A. 1993; Low-pH conformational changes of rabies virus glycoprotein and their role in membrane fusion. Journal of Virology 67:1365–1372
    [Google Scholar]
  13. Gilbertson R. L., Rojas M. R., Russell D. R., Maxwell D. P. 1991; Use of the asymmetric polymerase chain reaction and DNA sequencing to determine genetic variability of bean golden mosaic geminivirus in the Dominican Republic. Journal of General Virology 72:2843–2848
    [Google Scholar]
  14. Grigera P. R., Keil W., Wagner R. R. 1992; Disulfide-bonded discontinuous epitopes on the glycoprotein of vesicular stomatitis virus (New Jersey serotype). Journal of Virology 66:3749–3757
    [Google Scholar]
  15. Huang C., Chien M. S., Landolt M., Winton J. 1994; Characterization of the infectious hematopoietic necrosis vims glycoprotein using neutralizing monoclonal antibodies. Diseases of Aquatic Organisms IS29–35
    [Google Scholar]
  16. Kim C. H., Winton J. R., Leong J. C. 1994; Neutralization-resistant variants of infectious hematopoietic necrosis vims have altered vimlence and tissue tropism. Journal of Virology 68:8447–8453
    [Google Scholar]
  17. Koener J. F., Passavant C. W., Kurath G., Leong J. C. 1987; Nucleotide sequence of a cDNA clone carrying the glycoprotein gene of infectious hematopoietic necrosis vims, a fish rhabdovims. Journal of Virology 61:1342–1349
    [Google Scholar]
  18. LaFay F., Benmansour A., Chebli K., Flamand A. 1996; Immunodominant epitopes defined by a yeast-expressed library of random fragments of the rabies virus glycoprotein map outside major antigenic sites. Journal of General Virology 77:339–346
    [Google Scholar]
  19. Laver W. G., Air G. M., Webster R. G., Smith-Gill S. J. 1990; Epitopes on protein antigens: misconceptions and realities. Cell 61:553–556
    [Google Scholar]
  20. Luo L., Li Y., Snyder R. M., Wagner R. R. 1988; Point mutations in glycoprotein gene of vesicular stomatitis vims (New Jersey serotype) selected by resistance to neutralization by epitope-specific monoclonal antibodies. Virology 163:341–348
    [Google Scholar]
  21. Luo L., Li Y., Snyder R. M., Wagner R. R. 1990; Spontaneous mutations leading to antigenic variations in the glycoproteins of vesicular stomatitis virus field isolates. Virology 174:70–78
    [Google Scholar]
  22. Morzunov S. P., Winton J. R., Nichol S. T. 1995; The complete genome structure and phylogenetic relationship of infectious hematopoietic necrosis vims. Virus Research 38:175–192
    [Google Scholar]
  23. Mourich D. V., Leong J. C. 1991; Mapping the immunogenic regions of the IHNV glycoprotein in rainbow trout and mice. In Proceedings of the Second International Symposium on Viruses of Lower Vertebrates pp 93–100 Corvallis, Oregon, USA: Oregon State University;
    [Google Scholar]
  24. Nichol S. T., Rowe J. E., Fitch W. M. 1989; Glycoprotein evolution of vesicular stomatitis virus New Jersey. Virology 168:281–291
    [Google Scholar]
  25. Nichol S. T., Rowe J. E., Winton J. R. 1995; Molecular epizoo– tiology and evolution of the glycoprotein and nonvirion protein genes of infectious hematopoietic necrosis virus, a fish rhabdovirus. Virus Research 38:159–173
    [Google Scholar]
  26. Oshima K. H., Arakawa C. K., Higman K. H., Landolt M. L., Nichol S. T., Winton J. R. 1995; The genetic diversity and epizootiology of infectious hematopoietic necrosis virus. Virus Research 35:123–141
    [Google Scholar]
  27. Ping L., Lemon S. M. 1992; Antigenic structure of human hepatitis A virus defined by analysis of escape mutants selected against murine monoclonal antibodies. Journal of Virology 66:2208–2216
    [Google Scholar]
  28. Prehaud C., Coulon P., Lafay F., Thiers C., Flamand A. 1988; Antigenic site II of the rabies virus glycoprotein: structure and role in viral virulence. Journal of Virology 62:1–7
    [Google Scholar]
  29. Raux H., Coulon P., Lafay F., Flamand A. 1995; Monoclonal antibodies which recognize the acidic configuration of the rabies glycoprotein at the surface of the virion can be neutralizing. Virology 210:400–408
    [Google Scholar]
  30. Roberti K. A., Winton J. R., Rohovec J. S. 1991; Variants of infectious hematopoietic necrosis virus selected with glycoprotein– specific monoclonal antibodies. In Proceedings of the Second International Symposium on Viruses of Lower Vertebrates pp 33–42 Corvallis, Oregon, USA: Oregon State University;
    [Google Scholar]
  31. Sacramento D., Badrane H., Bourhy H., Tordo N. 1992; Molecular epidemiology of rabies virus in France: comparison with vaccine strains. Journal of General Virology 73:1149–1158
    [Google Scholar]
  32. Saito T., Taylor G., Laver W. G., Kawaoka Y., Webster R. G. 1994; Antigenicity of the N8 influenza A virus neuraminidase: existence of an epitope at the subunit interface of the neuraminidase. Journal of Virology 68:1790–1796
    [Google Scholar]
  33. Sanger F., Nicklen S., Coulson A. R. 1977; DNA sequencing with chain–terminating inhibitors. Proceedings of the National Academy of Sciences, USA 74:5463–5467
    [Google Scholar]
  34. Seif I., Coulon P., Rollin P. E., Flamand A. 1985; Rabies virulence: effect on pathogenicity and sequence characterization of rabies virus mutations affecting Site III of the glycoprotein. Journal of Virology 53:926–934
    [Google Scholar]
  35. Tulip W. R., Varghese J. N., Baker A. T., Van Donkelaar A., Laver W. G., Webster R. G., Colman P. M. 1991; Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants. Journal of Molecular Biology 22:122–148
    [Google Scholar]
  36. Vandepol S. B., LeFrancois L., Holland J. J. 1986; Sequences of the major antibody binding epitopes of the Indiana serotype of vesicular stomatitis virus. Virology 148:312–325
    [Google Scholar]
  37. VonHeijne H. 1986; A new method for predicting signal sequence cleavage sites. Nucleic Acids Research 14:4683–4690
    [Google Scholar]
  38. Webster R. G., Air G. M., Metzger D. W., Colman P. M., Varghese J. N., Baker A. T., Laver W. G. 1987; Antigenic structure and variation in an influenza virus N9 neuraminidase. Journal of Virology 61:2910–2916
    [Google Scholar]
  39. Whitt M. A., Buonocore L., Prehaud C., Rose J. K. 1991; Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein. Virology 185:681–688
    [Google Scholar]
  40. Winton J. R. 1991; Recent advances in detection and control of infectious hematopoietic necrosis virus in aquaculture. Annual Review of Fish Diseases 1:83–93
    [Google Scholar]
  41. Wolf K. 1988 Fish Viruses and Fish Viral Diseases pp 83–114 Ithaca: Cornell University Press;
    [Google Scholar]
  42. Xu L., Mourich D. V., Engelking H. M., Ristow S., Arnzen J., Leong J. C. 1991; Epitope mapping and characterization of infectious hematopoietic necrosis virus glycoprotein, using fusion proteins synthesized in Escherichia coli . Journal of Virology 65:1611–1615
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-77-12-3033
Loading
/content/journal/jgv/10.1099/0022-1317-77-12-3033
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error