1887

Abstract

A novel, linear B-cell epitope has been identified at the N terminus of the rabies virus (RABV) glycoprotein. Screening of a phage-display library demonstrated that two glycoprotein-specific mAbs recognized a conserved sequence, WxxxDI, which aligned between aa 14 and 19 of the mature glycoprotein. Screening of truncated glycoprotein fragments with both mAbs confirmed the location of the epitope in the N-terminal region. Alignment of amino acid sequences from a range of RABV isolates indicated that the site was conserved in most viruses. Alignment with representatives of other lyssaviruses suggested that it is conserved within phylogroup I, which includes the European bat lyssaviruses, but not phylogroup II. A 12 aa synthetic peptide of this epitope was recognized by both mAbs and sera from a subset of rabies-vaccinated dogs. In a multimeric form, the peptide could induce an epitope-specific response following immunization in rabbits and mice.

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2004-11-01
2024-04-18
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References

  1. Badrane H., Bahloul C., Perrin P., Tordo N. 2001; Evidence for two Lyssavirus phylogroups with distinct pathogenicity and immunogenicity. J Virol 75:3268–3276 [CrossRef]
    [Google Scholar]
  2. Cliquet F., Aubert M., Sagné L. 1998; Development of a fluorescent antibody virus neutralisation test (FAVN test) for the quantitation of rabies-neutralising antibody. J Immunol Methods 212:79–87 [CrossRef]
    [Google Scholar]
  3. Cliquet F., McElhinney L. M., Servat A., Boucher J. M., Lowings J. P., Goddard T., Mansfield K. L., Fooks A. R. 2004; Development of a qualitative indirect ELISA for the measurement of rabies virus-specific antibodies from vaccinated dogs and cats. J Virol Methods 117:1–8 [CrossRef]
    [Google Scholar]
  4. Coulon P., Lafay F., Flamand A. 1993; Rabies virus antigenicity: an overview. Onderstepoort J Vet Res 60:271–275
    [Google Scholar]
  5. Cox J. H., Dietzschold B., Schneider L. G. 1977; Rabies virus glycoprotein. II. Biological and serological characterization.. Infect Immun 16:754–759
    [Google Scholar]
  6. Dietzschold B., Wiktor T. J., Macfarlan R., Varrichio A. 1982; Antigenic structure of rabies virus glycoprotein: ordering and immunological characterization of the large CNBr cleavage fragments. J Virol 44:595–602
    [Google Scholar]
  7. 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. Proc Natl Acad Sci U S A 80:70–74 [CrossRef]
    [Google Scholar]
  8. Dietzschold B., Gore M., Marchadier D. 7 other authors 1990; Structural and immunological characterization of a linear virus-neutralizing epitope of the rabies virus glycoprotein and its possible use in a synthetic vaccine. J Virol 64:3804–3809
    [Google Scholar]
  9. Fooks A. R., McElhinney L. M., Brookes S. M., Johnson N., Keene V., Parsons G., Soldan A. 2002; Rabies antibody testing and the UK Pet Travel Scheme. Vet Rec 150:428–430
    [Google Scholar]
  10. Gaudin Y., Ruigrok R. W. H., Tuffereau C., Knossow M., Flamand A. 1992; Rabies virus glycoprotein is a trimer. Virology 187:627–632 [CrossRef]
    [Google Scholar]
  11. Gaudin Y., Raux H., Flamand A., Ruigrok R. W. H. 1996; Identification of amino acids controlling the low-pH-induced conformational change of rabies virus glycoprotein. J Virol 70:7371–7378
    [Google Scholar]
  12. Grabowska A., Jameson C., Laing P., Jeansson S., Sjögren-Jansson E., Taylor J., Cunningham A., Irving W. L. 1999; Identification of type-specific domains within glycoprotein G of herpes simplex virus type 2 (HSV-2) recognized by the majority of patients infected with HSV-2, but not by those infected with HSV-1. J Gen Virol 80:1789–1798
    [Google Scholar]
  13. Hooper D. C., Morimoto K., Bette M., Weihe E., Koprowski H., Dietzschold B. 1998; Collaboration of antibody and inflammation in clearance of rabies virus from the central nervous system. J Virol 72:3711–3719
    [Google Scholar]
  14. Inoue S., Motoi Y., Kashimura T., Ono K., Yamada A. 2003; Safe and easy monitoring of anti-rabies antibody in dogs using His-tagged recombinant N-protein. Jpn J Infect Dis 56:158–160
    [Google Scholar]
  15. Johnson N., Mansfield K. L., Fooks A. R. 2002a; Canine vaccine recipients recognize an immunodominant region of the rabies virus glycoprotein. J Gen Virol 83:2663–2669
    [Google Scholar]
  16. Johnson N., McElhinney L. M., Smith J., Lowings P., Fooks A. R. 2002b; Phylogenetic comparison of the genus Lyssavirus using distal coding sequences of the glycoprotein and nucleoprotein genes. Arch Virol 147:2111–2123 [CrossRef]
    [Google Scholar]
  17. Luo T. R., Minamoto N., Ito H., Goto H., Hiraga S., Ito N., Sugiyama M., Kinjo T. 1997; A virus-neutralizing epitope on the glycoprotein of rabies virus that contains Trp251 is a linear epitope. Virus Res 51:35–41 [CrossRef]
    [Google Scholar]
  18. Ma B., Elkayam T., Wolfson H., Nussinov R. 2003; Protein–protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces. Proc Natl Acad Sci U S A 100:5772–5777 [CrossRef]
    [Google Scholar]
  19. Ni Y., Tominaga Y., Honda Y., Morimoto K., Sakamoto S., Kawai A. 1995; Mapping and characterization of a sequential epitope on the rabies virus glycoprotein which is recognized by a neutralizing monoclonal antibody, RG719. Microbiol Immunol 39:693–702 [CrossRef]
    [Google Scholar]
  20. 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. J Virol 62:1–7
    [Google Scholar]
  21. 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 [CrossRef]
    [Google Scholar]
  22. Roche S., Gaudin Y. 2002; Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers. Virology 297:128–135 [CrossRef]
    [Google Scholar]
  23. Seif I., Coulon P., Rollin P. E., Flamand A. 1985; Rabies virulence: effect on pathogenicity and sequence characterization of rabies virus mutations affecting antigenic site III of the glycoprotein. J Virol 53:926–934
    [Google Scholar]
  24. Smith G. P., Scott J. K. 1993; Libraries of peptides and proteins displayed on filamentous phage. Methods Enzymol 217:228–257
    [Google Scholar]
  25. Smith R. A., Myers N. B., Robinson M., Hansen T. H., Lee D. R. 2002; Polymorphism at position 97 in MHC class I molecules affects peptide specificity, cell surface stability, and affinity for β 2-microglobulin. J Immunol 169:3105–3111 [CrossRef]
    [Google Scholar]
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