Skip to main content
Log in

Activation of the alternative complement pathway by mumps infected cells: Relationship to viral neuraminidase activity

  • Original Papers
  • Published:
Archives of Virology Aims and scope Submit manuscript

Summary

An inverse relationship exists between the sialic acid content of a particle and its ability to activate the alternative complement pathway. The present studies were performed to determine if the neuraminidase (NANase) activities of different mumps virus strains could influence the ability of mumps virus infected cells to activate the alternative pathway. CV-1 cells were infected with three different mumps virus strains (RW, O'Take, and Kilham) and after 24 hours, 10 percent guinea pig serum (GPS) treated with EGTA/MgCl2 or GPS lacking the 4th component of complement (C4DGPS) was added to the cell monolayers. After 30 minutes, the percentage C3 consumed was determined by a functional hemolytic assay. Cells infected with RW (high NANase) consumed significantly more C3 (23.2 per cent) than cells infected with Kilham (5.7 percent, low NANase). Cells infected with O'Take were intermediate in their ability to activate C3. The degree of C3 deposition on the surface of infected cells, detected by fluorescence microscopy, was also greater for cells infected with the RW than the Kilham strain of mumps virus. These studies suggest that the NANase activity of mumps virus can influence the ability of infected cells to activate the alternative pathway and thereby, the ability of complement to participate in host defense against mumps virus infection.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Ellman, L., Green, I., Frank, M.: Genetically controlled complete deficiency of the fourth component of complement in the guinea pig. Science170, 74–75 (1970).

    Google Scholar 

  2. Fearon, D. T.: Regulation by membrane sialic acid of B1H-dependent decay-dissociation of amplification C3 convertase of the alternative complement pathway. Proc. Nat. Acad. Sci. (U.S.A.)75, 1791–1794 (1978).

    Google Scholar 

  3. Hirsch, R. L.: The Complement System: Its importance in the host response to viral infection. Microbiol. Rev.46, 71–85 (1982).

    Google Scholar 

  4. Hirsch, R. L., Winkelstein, J. A., Griffin, D. E.: The role of complement in viral infections. III. Activation of the classical and alternative pathways by Sindbis virus. J. Immunol.124, 2507–2510 (1980).

    Google Scholar 

  5. Hirsch, R. L., Griffin, D. E., Winkelstein, J. A.: Host modification of Sindbis virus sialic acid content influences alternative complement pathway activation and virus clearance. J. Immunol.127, 1740–1743 (1981).

    Google Scholar 

  6. Hirsch, R. L., Griffin, D. E., Winkelstein, J. A.: Natural immunity to Sindbis virus is influenced by host tissue sialic acid content. Proc. Nat. Acad. Sci. (U.S.A.)80, 548–550, (1983).

    Google Scholar 

  7. Kabat, E., Mayer, M. M.: Kabat und Mayer's Experimental Immunochemistry, 2nd ed., 133–240. Springfield, Ill.: Charles C Thomas, 1967.

    Google Scholar 

  8. Kazatchkine, M. D., Fearon, D. T., Austen, K. F.: Human alternative complement pathway: Membrane-associated sialic acid regulates the competition between B and B1H for cell bound C3b. J. Immunol.122, 75–81 (1979).

    Google Scholar 

  9. Lambre, C. R., Kazatchkine, M. D., Maillet, F., Thibon, M.: Guinea pig erythrocytes, after their contact with influenza virus, acquire the ability to activate the human alternative pathway through virus-induced desialation of the cells. J. Immunol.126, 629–634 (1982).

    Google Scholar 

  10. McCarthy, M., Jubelt, B., Fay, D. B., Johnson, R. T.: Comparative studies of five mumps strainsin vitro and in neonatal hamsters: evaluation of growth, cytopathogenecity, and neurovirulence. J. Med. Virol.5, 1–15 (1980).

    Google Scholar 

  11. McSharry, J. J., Pickering, R. J., Caliguiri, L. A.: Activation of the alternative pathway by enveloped viruses containing limited amounts of sialic acid. Virology114, 507–515 (1981).

    Google Scholar 

  12. Merz, D. C., Wolinsky, J. S.: Biochemical features of mumps virus neuraminidases and their relationship with pathogenicity. Virology114, 218–227 (1981).

    Google Scholar 

  13. Oldstone, M. B. A., Lampert, R. N.: Antibody mediated complement dependent lysis of virus infected cells. Springer Seminars in Immunopathology, Vol. 2, 261–283 (1979).

    Google Scholar 

  14. Server, A. C., Merz, D. C., Waxham, M. N., Wolinsky, J. S.: Differentiation of mumps virus strains with monoclonal antibody to the HN glycoprotein. Infect. Immun.35, 179–186 (1982).

    Google Scholar 

  15. Stollar, V., Stollar, B. D., Koo, R., Harrap, K. A., Schlesinger, R. W.: Sialic acid content of Sindbis virus from vertebrate and mosquito cells. Equivalence of biological and immunological viral properties. Virology69, 104–115 (1976).

    Google Scholar 

  16. Warren, L.: The thiobarbituric acid assay of sialic acids. J. Biol. Chem.234, 1971–1975 (1961).

    Google Scholar 

  17. Welsh, R. M.: Host cell modification of lymphocytic choriomeningitis virus and New Castle disease virus altering viral inactivation by human complement. J. Immunol.118, 348–354 (1977).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

With 1 Figure

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hirsch, R.L., Wolinsky, J.S. & Winkelstein, J.A. Activation of the alternative complement pathway by mumps infected cells: Relationship to viral neuraminidase activity. Archives of Virology 87, 181–190 (1986). https://doi.org/10.1007/BF01315298

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01315298

Keywords

Navigation