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Related Experiment Videos

Influenza virus ISCOMs: biochemical characterization.

B Sundquist1, K Lövgren, S Höglund

  • 1National Veterinary Institute, Division of Vaccine Research, Uppsala, Sweden.

Vaccine
|February 1, 1988
PubMed
Summary

Immunostimulating complexes (ISCOMs) were created using influenza A virus glycoproteins (HA/NA) and Quil A. These cage-like structures preserve the biological activity of HA and NA, showing potential for vaccine development.

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Area of Science:

  • Biochemistry
  • Virology
  • Immunology

Background:

  • Influenza A virus envelope glycoproteins, haemagglutinin (HA) and neuraminidase (NA), are key targets for vaccines.
  • Immunostimulating complexes (ISCOMs) are novel vaccine delivery systems with potential for enhanced immunogenicity.

Purpose of the Study:

  • To prepare and characterize ISCOMs derived from influenza A virus HA and NA glycoproteins.
  • To assess the structural integrity and biological activity of HA and NA within ISCOMs.

Main Methods:

  • ISCOMs were formulated using influenza A virus HA and NA glycoproteins complexed with the saponin Quil A.
  • Morphological characterization was performed using electron microscopy.
  • Sedimentation analysis was employed to determine the size and structure of ISCOMs and glycoprotein micelles.

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  • Biological activity of HA and NA was assessed post-formulation.

    • Main Results:

    • ISCOMs were successfully prepared, exhibiting symmetrical cage-like structures approximately 40 nm in diameter.
    • Quil A constituted 5% of the ISCOM protein content.
    • ISCOMs displayed a sedimentation coefficient of approximately 19 S, distinct from glycoprotein micelles (30 S).
    • The biological activities of both HA and NA were retained in the ISCOM formulation.

    Conclusions:

    • Influenza A virus HA and NA can be effectively incorporated into ISCOMs.
    • ISCOMs maintain the structural and functional integrity of viral glycoproteins.
    • These findings support the potential of ISCOMs as effective vaccine platforms for influenza A.