Medical Microbiology and Immunology

, Volume 166, Issue 1–4, pp 165–171 | Cite as

Detection of antigenic variation in influenza virus neuraminidase by the ESSEN-NIT and the WHO standard procedure

  • Jürgen Werner
  • Olaf Thraenhart
  • Ernst Kuwert


A new rapid modified micro-neuraminidase-inhibition test (ESSEN-NIT) has recently been described. This test was originally devised to facilitate largescale screening for serum antibodies to influenza virus neuraminidase. It was shown that this test yielded results comparable to those obtained with the WHO standard procedure.

Our report presents data on the comparison between the WHO method and the ESSEN-NIT with respect to their capability in detecting antigenic differences in neuraminidase of various strains of influenza A viruses belonging to the H3N2 subtype family. Two antiserums against the N2 antigens of the A/Hongkong/1/68 (X15HK) and of the A/Port Chalmers/1/73 (X42) recombinant strains were used in characterization experiments. The results obtained indicate that the ESSEN-NIT is at least as sensitive in detecting antigenic variations of neuraminidase as the WHO standard procedure. The drift of the N2 enzyme which occurred as early as 1969 and is known to continue to date, could be clearly demonstrated. Major and minor antigenic changes of neuraminidase in representative influenza isolates were equally well detected by both assays.

The ESSEN-NIT offers the advantage of speed, economy, and computerized evalutaion of data.


Influenza Standard Procedure Influenza Virus Recombinant Strain Serum Antibody 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Aminoff, D.: Methods for the quantitative estimation of N-acetylneuramic acid and their application to hydrolysates of sialomucoids. Biochem. J.81, 384–392 (1961)PubMedGoogle Scholar
  2. 2.
    Aymard-Henry, M., Colemann, M.T., Dowdle, W.R., Laver, W.G., Webster, R.G.: Influenza virus neuraminidase and neuraminidase-inhibition test procedures. Bull. WHO48, 199–202 (1973)PubMedGoogle Scholar
  3. 3.
    Chakraverty, P.: Antigenic relationships between the neuraminidase of influenza B virus. Bull. WHO46, 473–476 (1972)PubMedGoogle Scholar
  4. 4.
    Drzeniek, R.: Wechselwirkungen zwischen Myxoviren und Zelloberflächen. III Neuraminidase der Myxoviren. Z. med. Mikrobiol. u. Immunol.156, 1–30 (1970)Google Scholar
  5. 5.
    Paniker, C.K.J.: Serological relationships between the neuraminidases of influenza viruses. J. Gen. Virol.2, 385–394 (1968)PubMedGoogle Scholar
  6. 6.
    Rott, R., Becht, R. Orlich, M.: Antigenic relationships between the surface antigens of avian and equine influenza viruses. Med. Microbiol. Immunol.161, 253–261 (1975)PubMedGoogle Scholar
  7. 7.
    Schild, G.C., Newman, R.W.: Immunological relationships between the neuraminidase of human and animal influenza viruses. Bull. WHO,41, 437–445 (1969)PubMedGoogle Scholar
  8. 8.
    Schild, G.C., Henry-Aymard, M., Pereira, M.S., Chakraverty, P., Dowdle, W., Coleman, M., Chang, W.K.: Antigenic variation in current human type A influenza viruses: Antigenic characteristics of the variants and their geographic distribution. Bull. WHO,48, 269–278 (1973)PubMedGoogle Scholar
  9. 9.
    Schild, G.C., Oxford, J.S., Dowdle, W.R., Coleman, M., Pereira, M.S., Chakraverty, P.: Antigenic variation in current influenza viruses: evidence for a high frequency of antigenic ‘drift’ for the Hongkong virus. Bull. WHO,51, 1–11 (1974)PubMedGoogle Scholar
  10. 10.
    Schulman, J.L., Kilbourne, E.D.: The antigenic relationship of the neuraminidase of Hongkong virus to that of other human strains of influenza A virus. Bull. WHO41, 425–428 (1969)PubMedGoogle Scholar
  11. 11.
    Schulman, J.L., Kilbourne, E.D.: The antigenic relationship of the neuraminidase and neuraminidase antigens of influenza virus: Distinctiveness of hemagglutinin antigen of Hongkong virus. Proc. Nat. Acad. Sci.63, 326–333 (1969)PubMedGoogle Scholar
  12. 12.
    Siekamnn, U., Schoop, H.J., Kuwert, E.: Contribution to the standardization for influenza neuraminidase inhibition tests, based on enzyme-antienzyme kinetic studies. Dev. Biol. Stand.28, 324–335 (1975)PubMedGoogle Scholar
  13. 13.
    Thraenhart, O., Kuwert, E.K.: Standardization of a rapid modified micro-neuraminidase-inhibition test (Essen-NIT) for influenza virus-neuraminidase antibody assay and comparison with the W.H.O. method. J. Biol. Stand.4, 225–241 (1976)PubMedGoogle Scholar
  14. 14.
    Thraenhart, O., Kuwert, E.K.: Rapid enzymologic anti-neuraminidase antibody microtest. Dev. Biol. Stand.39, 475–480 (1977)Google Scholar
  15. 15.
    Warren, L.: The thiobarbituric acid assay of sialic acids. J. Biol. Chem.234, 1971–1975 (1959)PubMedGoogle Scholar
  16. 16.
    Webster, R.G., Pereira, H.G.: A common surface antigen in influenza viruses from human and avian sources. J. Gen. Virol.3, 201–208 (1968)PubMedGoogle Scholar
  17. 17.
    Webster, R.G., Campbell, C.H.: An inhibition test for identifying the neuraminidase antigen on influenza viruses. Avian Dis.16, 1057–1066 (1972)PubMedGoogle Scholar
  18. 18.
    Werner, J., Schudrowitz, C., Köhler, H.: Antigenic variation of neuraminidase of human type A influenza (H3N2) viruses isolated in Berlin (West). Zbl. Bakt. Hyg., Abt. Orig. A233, 440–446 (1975)Google Scholar
  19. 19.
    WHO Report: A revised System of nomenclature for influenza viruses. Bull. WHO45, 119–124 (1972)Google Scholar

Copyright information

© Springer-Verlag 1978

Authors and Affiliations

  • Jürgen Werner
    • 1
  • Olaf Thraenhart
    • 1
  • Ernst Kuwert
    • 1
  1. 1.Institut für Medizinische Virologie und ImmunologieUniversität Essen-GesamthochschuleEssen 1Federal Republic of Germany

Personalised recommendations