Immunoelectron microscopy of influenza A virus neuraminidase glycoprotein topography Free

Abstract

Using immunoelectron microscopy, the distribution of influenza A virus neuraminidase (NA) glycoproteins was examined, after performing immunoreactions to virions on the grid. With polyclonal antibody, the immunolabels of the glycoproteins were found to be homogeneously distributed, whereas with monoclonal antibody they were found to be distributed in clusters. After destruction of haemagglutinin (HA) but not of NA activity with a high concentration of trypsin, the remaining visible spikes were evenly distributed. This finding was consistent with the absence of immunolabelling with anti-HA antibody, and the homogeneous pattern of immunolabels with anti-NA polyclonal antibody, but not with the clustered labelling with the anti-NA monoclonal antibody. Thus, the immunolabelling image with anti-NA polyclonal antibody was considered to reflect the true one.

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1992-08-01
2024-03-28
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References

  1. Aminoff D. 1961; Methods of the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochemical Journal 81:384–391
    [Google Scholar]
  2. de Petris S. 1977; Distribution and mobility of plasma membrane components on lymphocytes. In Cell Surface Reviews vol 3 pp. 643–728 Edited byt Post G., Nicolson G. L. Amsterdam: Elsevier;
    [Google Scholar]
  3. Erickson A. H., Kilbourne E. D. 1980; Mutation in the hemagglutinin of A/N-WS/33 influenza virus recombinants influencing sensitivity to trypsin and antigenic reactivity. Virology 107:320–330
    [Google Scholar]
  4. Hernandez F., Rivera P., Hosaka Y. 1987; Homogeneous distributions of parainfluenza virus glycoproteins demonstrated by immunogold-labelling and light staining with uranyl acetate in electron microscopy. Journal of Virological Methods 15:273–277
    [Google Scholar]
  5. Jackson D. C., Crabb B. S., Poumbourios P., Tulip W. R., Laver W. G. 1991; Three antibody molecules can bind simultaneously to each monomer of the tetramer of influenza virus neuraminidase and the trimer of influenza virus hemagglutinin. Archives of Virology 116:45–56
    [Google Scholar]
  6. Lamb R. A., Choppin P. W. 1976; Synthesis of influenza virus proteins in infected cells: translation of viral peptides, including three P polypeptides, from RNA produced by primary transcription. Virology 74:504–519
    [Google Scholar]
  7. Laver W. G., Kilbourne E. D. 1966; Identification in a recombinant influenza virus of structural proteins derived from both parents. Virology 30:493–501
    [Google Scholar]
  8. Murti K. G., Webster R. G. 1986; Distributions of hemagglutinin and neuraminidase on influenza virions as revealed by immunoelectron microscopy. Virology 149:36–43
    [Google Scholar]
  9. Poumbourios P., Brown L. E., White D. O., Jackson D. C. 1990; The stoichiometry of binding between monoclonal antibody molecules and the hemagglutinin of influenza virus. Virology 179:768–776
    [Google Scholar]
  10. Seto J. T., Rott R. 1966; Functional significance of sialidase during influenza virus multiplication. Virology 30:731–740
    [Google Scholar]
  11. Singer S. L., Nicolson G. L. 1972; The fluid mosaic model of the structure of cell membranes. Science 175:720–731
    [Google Scholar]
  12. Taylor H. P., Armstrong S. J., Dimmock N. J. 1987; Quantitative relationships between an influenza virus and neutralizing antibody. Virology 159:288–298
    [Google Scholar]
  13. Tiffany J. M., Blough H. A. 1970; Estimation of the number of surface projections on myxo- and paramyxoviruses. Virology 41:392–394
    [Google Scholar]
  14. Tulloch P. A., Colman P. M., Davis P. C., Laver W. G., Webster R. G., Air G. M. 1986; Electron and X-ray diffraction studies of influenza neuraminidase complexed with monoclonal antibodies. Journal of Biology 190:215–225
    [Google Scholar]
  15. Wrigley N. G., Laver W. G., Downie J. C. 1977; Binding of antibodies to isolated haemagglutinin and neuraminidase molecules of influenza virus observed in the electron microscope. Journal of Molecular Biology 109:405–421
    [Google Scholar]
  16. Wrigley N. G., Brown E. B., Daniels R. S., Douglas A. R., Skehel J. J., Wiley D. C. 1983; Electron microscopy of influenza haemagglutinin-monoclonal antibody complexes. Virology 131:308–314
    [Google Scholar]
  17. Yewdell J. W., Gerhard W., Bächi T. 1983; Monoclonal antihemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/8/34-mediated hemolysis. Journal of Virology 48239–248
    [Google Scholar]
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