1887

Abstract

Virus-neutralizing activity of two monoclonal antibodies (mAbs), #7-1-9 and #1-46-12, against rabies virus glycoprotein (G) was compared. Although these mAbs affected the virion’s ability to bind to host cells similarly, a big difference was found in the titres of virus neutralization (1:7132 and 1:32 for mAbs #1-46-12 and #7-1-9, respectively, at a concentration of 10 μg protein/ml). Although no big difference in virion-binding affinity between the two mAbs was found, the number of antibodies required for virus neutralization was very low, ⩽20 molecules for mAb #1-46-12 and ⩾250 molecules for mAb #7-1-9. In the latter case, the mAbs cover a major part of the virion surface and cause steric hindrance of viral receptor-binding activity. The infectivity of an epitope-preserved escape mutant virus (R-61) was not affected by the binding of high numbers of mAb #1-46-12 to the virion, which implies that mAb binding does not mask the receptor-binding site of the viral spikes. Based on these results, it is hypothesized that mAb #1-46-12 affected virus infectivity by a mechanism different from covering the virion spikes. Possible virus-neutralizing mechanisms by low numbers of mAb #1-46-12 in comparison to that of mAb #7-1-9 are discussed.

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2002-12-01
2020-12-03
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References

  1. Anzai J., Takamatsu F., Takeuchi K., Kohno T., Morimoto K., Goto H., Minamoto N., Kawai A.. 1997; Identification of a phosphatase-sensitive epitope of rabies virus nucleoprotein which is recognized by a monoclonal antibody 5-2-26. Microbiology and Immunology41:229–240
    [Google Scholar]
  2. Barroso I., Santisteban P.. 1999; Insulin-induced early growth response gene (Egr-1) mediates a short term repression of rat malic enzyme gene transcription. Journal of Biological Chemistry247:17997–18004
    [Google Scholar]
  3. Burton D. R., Saphire E. O., Parren P. W. H. I.. 2001; A model for neutralization of viruses based on antibody coating of the virion surface. Current Topics in Microbiology and Immunology260:109–143
    [Google Scholar]
  4. Coll J. M.. 1995; The glycoprotein G of rhabdoviruses. Archives of Virology140:827–851
    [Google Scholar]
  5. Colonno R. J., Callahan P. L., Leippe D. M., Rueckert R. R., Tomassini J. E.. 1989; Inhibition of rhinovirus attachment by neutralizing monoclonal antibodies and their Fab fragments. Journal of Virology63:36–42
    [Google Scholar]
  6. Coulon P., Rollin P. E., Flamand A.. 1982; Molecular basis of rabies virus virulence. II. Identification of a site on the CVS glycoprotein associated with virulence. Journal of General Virology64:693–696
    [Google Scholar]
  7. Coulon P., Rollin P. E., Aubert M., Flamand A.. 1983; Molecular basis of rabies virus virulence. I. Selection of avirulent mutants of the CVS strain with anti-G monoclonal antibodies. Journal of General Virology61:97–100
    [Google Scholar]
  8. Dietzschold B., Cox J. H., Schneider L. G.. 1979; Rabies virus strains: a comparison study by polypeptide analysis of vaccine strains with different pathogenic patterns. Virology98:63–75
    [Google Scholar]
  9. 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, USA80:70–74
    [Google Scholar]
  10. Dietzschold B., Rupprecht C. E., Tollis M., Lafon M., Mattei J., Wiktor T. J., Koprowski H.. 1988; Antigenic diversity of the glycoprotein and nucleocapsid protein of rabies and rabies-related viruses: implications for epidemiology and control of rabies. Reviews of Infectious Diseases10 (Suppl. 4):785–798
    [Google Scholar]
  11. Dietzschold B., Gore M., Marchadier D., Niu H. S., Bunschoten H. M., Otvos L. Jr, Wunner W. H., Ertl H. C., 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 Virology64:3804–3809
    [Google Scholar]
  12. Flamand A., Wiktor T. J., Koprowski H.. 1980; Use of hybridoma monoclonal antibodies in the detection of antigenic differences between rabies and rabies-related virus proteins. II. The glycoprotein. Journal of General Virology48:105–109
    [Google Scholar]
  13. Flamand A., Raux H., Gaudin Y., Ruigrok R. W.. 1993; Mechanism of rabies virus neutralization. Virology194:302–313
    [Google Scholar]
  14. Hirai K., Kawano H., Mifune K., Fujii H., Nishizono A., Shichijo A., Mannen K.. 1992; Suppression of cell-mediated immunity by street rabies virus infection. Microbiology and Immunology36:1277–1290
    [Google Scholar]
  15. Irie T., Matsuda Y., Honda Y., Morimoto K., Kawai A.. 2002; Studies on the escape mutants of rabies virus which are resistant to the neutralization by a highly conserved conformational epitope-specific monoclonal antibody #1-46-12. Microbiology and Immunology47:449–461
    [Google Scholar]
  16. Kawai A.. 1977; Transcriptase activity associated with rabies virion. Journal of Virology24:826–835
    [Google Scholar]
  17. Kawai A., Takeuchi K.. 1992; Temperature-sensitivity of the replication of rabies virus (HEP-Flury strain) in BHK-21 cells. I. Alteration of viral RNA synthesis at the elevated temperature. Virology186:524–532
    [Google Scholar]
  18. Kawai A., Morimoto K.. 1994; Functional aspects of lyssavirus proteins. Current Topics in Microbiology and Immunology187:27–42
    [Google Scholar]
  19. Kawai A., Anzai J., Honda Y., Morimoto K., Takeuchi K., Kohno T., Wakisaka K., Goto H., Minamoto N.. 1997; Monoclonal antibody #5-2-26 recognizes the phosphatase-sensitive epitope of rabies virus nucleoprotein. Microbiology and Immunology41:33–42
    [Google Scholar]
  20. Lafon M.. 1994; Immunobiology of lyssaviruses: the basis for immunoprotection. Current Topics in Microbiology and Immunology187:145–160
    [Google Scholar]
  21. Lafon M., Wiktor T. J., Macfarlan R. I.. 1983; Antigenic sites on the CVS rabies virus glycoprotein: analysis with monoclonal antibodies. Journal of General Virology64:843–851
    [Google Scholar]
  22. Louie R. E., Dobkin M. B., Meyer P., Chin B., Roby R. E., Hammar A. H., Cabasso V. J.. 1975; Measurement of rabies antibody: comparison of the mouse neutralization test (MNT) with the rapid fluorescent focus inhibition test (RFFIT). Journal of Biological Standardization3:365–373
    [Google Scholar]
  23. Morimoto K., Kawai A., Mifune K.. 1992; Comparison of rabies virus G proteins produced by cDNA-transfected animal cells that display either inducible or constitutive expression of the gene. Journal of General Virology73:335–345
    [Google Scholar]
  24. Nakahara K., Ohnuma H., Sugita S., Yasuoka K., Nakahara T., Tochikura T. S., Kawai A.. 1999; Intracellular behavior of rabies virus matrix protein (M) is determined by the viral glycoprotein (G). Microbiology and Immunology43:259–270
    [Google Scholar]
  25. 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. Microbiology and Immunology39:693–702
    [Google Scholar]
  26. Perrin P., Tino de Franco M., Jallet C., Fouque F., Morgeaux S., Tordo N., Colle J. H.. 1996; The antigen-specific cell-mediated immune response in mice is suppressed by infection with pathogenic lyssaviruses. Research in Virology147:289–299
    [Google Scholar]
  27. Possee R. D., Schild G. C., Dimmock N. J.. 1982; Studies on the mechanism of neutralization of influenza virus by antibody: evidence that neutralizing antibody (anti-haemagglutinin) inactivates influenza virus in vivo by inhibiting virion transcriptase activity. Journal of Virology58:373–386
    [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 Virology62:1–7
    [Google Scholar]
  29. Rando R. F., Notkins A. L.. 1994; Production of human monoclonal antibodies against rabies virus. Current Topics in Microbiology and Immunology187:195–205
    [Google Scholar]
  30. Sakamoto S., Ide T., Nakatake H., Tokiyoshi S., Yamamoto M., Kawai A., Smith J. S.. 1994; Studies on the antigenicity and nucleotide sequence of the rabies virus Nishigahara strain, a current seed strain used for dog vaccine production in Japan. Virus Genes8:35–46
    [Google Scholar]
  31. 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. Journal of Virology53:926–934
    [Google Scholar]
  32. Thraenhart O., Marcus I., Kreuzfelder E.. 1994; Current and future immunoprophylaxis against human rabies: reduction of treatment failures and errors. Current Topics in Microbiology and Immunology187:173–194
    [Google Scholar]
  33. Wiktor T. J., Gyorgy E., Schlumberger D., Sokol F., Koprowski H.. 1973; Antigenic properties of rabies virus components. Journal of Immunology110:269–276
    [Google Scholar]
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