Advertisement

QS-21 Augments the Antibody Response to a Synthetic Peptide Vaccine Compared to Alum

  • J. E. Kirkley
  • Paul H. Naylor
  • Dante J. Marciani
  • Charlotte R. Kensil
  • Mark Newman
  • A. L. Goldstein

Abstract

The immunomodulating ability of adjuvants has been shown to enhance immune responses directed both specifically and non-specifically against tumor development and growth and to increase immune response to weak antigens. This study compared two adjuvants, alum and QS-21, given separately and together in a candidate p17-based subunit AIDS vaccine, HGP-30-KLH. Alum, the only adjuvant approved for human use, confers a particulate appearance to the immunogen by adsorbing it and retains the immunogen in the body.1 QS-21 is a pure triterpene glycoside saponin adjuvant,2 and is purified from the total saponin fraction of Quillaja saponaria Molina. Crude mixtures of Quillaja saponaria saponins serve as the matrix component of the immunostimulating complex (ISCOM).3 The study’s hypothesis was that these two adjuvants function by different means to increase antibody titer to a synthetic peptide immunogen. QS-21, with its biochemical as well as physical properties, was expected to generate a greater antibody response than alum, and the two combined may be additive or synergistic.

Keywords

Human Immunodeficiency Virus Human Immunodeficiency Virus Type Average Optical Density Human Immunodeficiency Virus Vaccine Increase Antibody Titer 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Warren, H.S., Vogel, F.R., and Chedid, L.A., ‘Current status of immunological adjuvants,’ Ann. Rev. Immun. 4:369–388, 1986.CrossRefGoogle Scholar
  2. 2.
    Kensil, C.R., Patel, U., Lennick, M., and Marciani, D., “Separation and characterization of saponins with adjuvant activity from Quillaja saponaria Molina cortex,” J. Immunology 146:431–437, 1991.Google Scholar
  3. 3.
    Morein, B., Sundquist, B., Hoglund, S., Dalsgaard, K., and Osterhaus, A., ‘Iscom, a novel structure for antigenic presentation of membrane proteins from enveloped viruses,’ Nature 308:457, 1984.PubMedCrossRefGoogle Scholar
  4. 4.
    Coates, A.R.M., Cookson, J., Barton, G.J., Zvelebil, M.H., and Sternberg, M.J., ‘AIDS vaccine predictions,’ Nature 326:549–550, 1987.PubMedCrossRefGoogle Scholar
  5. 5.
    Jaing, J.D., Chu, F.N., Naylor, P., Kirkley, J., Mandelli, J., Wallace, J.I., Sarin, P., Goldstein, A., and Bekesi, J.G., ‘Antibody responses to synthetic epitopes of HIV-1 gag p17 in different stages of HIV-1 infection in homosexuals and IV drug abusers,’ Proc. Natl. Acad. Sci. (submitted).Google Scholar
  6. 6.
    Wahren, B., Rosen, J., Sandstrom, E., Mathiesen, T., Modrow, S., and Wigzell, H., ‘HIV-1 peptides induce a proliferative response in lymphocytes from infected persons,’ J. AIDS 4:448–456, 1989.Google Scholar
  7. 7.
    Achour, A., Picard, O., Zagury, D., Sarin, P.S., Gallo, R.C., Naylor, P.H., and Goldstein, A.L., ‘HGP-30, a synthetic analogue of human immunodeficiency virus (HIV) p17, is a target for cytotoxic lymphocytes in HIV-infected individuals,’ PNAS 87:7045–7049, 1990.PubMedCrossRefGoogle Scholar
  8. 8.
    Goldstein, A.L., Naylor, P.H., Sarin, P.S., Kirkley, J.E., Stambuk, D., and Rios, A., ‘Progress in the development of a p17 based HIV vaccine: immunogenicity of HGP-30 in humans,’ Abstract S.A.76, VI International Conference on AIDS, San Francisco, Calif., U.S.A., 1990.Google Scholar
  9. 9.
    Boucher, A.B., Krone, W.J.A., Goudsmit, J., Meloen, R.H., Naylor, P.H., Goldstein, A.L., Sun, D.K., and Sarin, P.S., ‘Immune response and epitope mapping of a candidate HIV p17 vaccine HGP-30,’ J. Clin. Lab. An. 4:43–47, 1990.CrossRefGoogle Scholar
  10. 10.
    Papsidero, L.D., Sheu, M., and Ruscetti, F.W., ‘Human immunodeficiency virus type 1 neutralizing monoclonal antibodies which react with p17 core protein. Characterization and epitope mapping,’ J. Virol. 63:267–272, 1989.PubMedGoogle Scholar
  11. 11.
    Goldstein, A.L., Naylor, P.H., Kirkley, J.E., Naylor, C.W., Gibbs, C.J., and Sarin, P.S., ‘Evaluation of a synthetic HIV-1 p17-based candidate AIDS vaccine, HGP-30,’ Abstract M.C.P.13, V International Conference on AIDS, Montreal, Quebec, Canada, 1989.Google Scholar
  12. 12.
    Naylor, P.H., Naylor, C.W., Badamchian, M., Wada, S., Goldstein, A.L., Wang, S.-S., Sun, D., Thorton, A.H., and Sarin, P., ‘Human immunodeficiency virus containing an epitope immunoreactive with thymosin alpha 1 and the thirty amino acid synthetic p17 group specific antigen peptide HGP30,’ PNAS 84:2951–2955, 1986.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • J. E. Kirkley
    • 1
  • Paul H. Naylor
    • 1
  • Dante J. Marciani
    • 2
  • Charlotte R. Kensil
    • 2
  • Mark Newman
    • 2
  • A. L. Goldstein
    • 1
  1. 1.Dept. of Biochemistry and Molecular BiologyThe George Washington University Medical CenterUSA
  2. 2.Cambridge Biotech Corp.WorcesterUSA

Personalised recommendations