HIV Protocols pp 265-271 | Cite as

Analysis of Antibody Interactions with HIV-1 Envelope Expressed on the Surface of Acutely Infected H9 Cells

  • Thomas C. VanCott
  • Paul L. Hallberg
Part of the Methods in Molecular Medicine™ book series (MIMM, volume 17)


Protective antibody responses against HIV-1 have yet to be identified or determined. HIV-1 envelope gpl20/gp41 is known to exist as a multimer (tetramers or trimers) on the surface of the virion (1, 2, 3, 4). A number of immunoassays have been developed to evaluate HIV-1-specific binding antibody responses using peptides, fusion proteins, and recombinant proteins. Attempts to correlate antibody binding parameters with in vitro HIV-1 neutralization capacity have identified correlations between the presence of V3 antibodies and the capacity to neutralize T-cell line adapted strains of HIV-1. However, no correlation with neutralization of primary HIV-1 isolates and v3 antibodies have been identified (5). Furthermore, binding to monomeric forms of gpl20 has shown little correlation with neutralization of the homologous primary HIV-1 indicating that epitope accessibility and tertiary structure of monomeric forms of gpl20 differs from quaternary structure of membrane expressed oligomeric gpl20/gp41 (6, 7, 8).


Normal Human Serum Negative Control Seron Protective Antibody Response Microsphere Particle Calibrite Bead 
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  1. 1.
    Doms, R. W., Earl, P. L., and Moss, B. (1991) The assembly of the HIV-1 env glycoprotein into dimers and tetramers. Adv. Exp. Med. Biol. 300, 203–219.PubMedGoogle Scholar
  2. 2.
    Earl, P. L., Doms, R. W., and Moss, B. (1990) Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein. Proc. Natl. Acad. Sci. USA 87, 648–652.PubMedCrossRefGoogle Scholar
  3. 3.
    Pinter, A., Honnen, W. J., Tilley, S. A., Bona, C., Zaghouani, H., Gorny, M., and Zolla-Pazner, S. (1989) Oligomeric structure of gp41, the transmembrane protein of human immunodeficiency virus type 1. J. Virol. 63, 2674–2679.PubMedGoogle Scholar
  4. 4.
    Schawaller, M., Smith, C. E., Skehel, J. J., and Wiley, D. C. (1989) Studies with cross-linking reagents on the oligomeric structure of the env-glycoprotein of HIV. Virology 172, 367–369.PubMedCrossRefGoogle Scholar
  5. 5.
    VanCott, T. C., Polonis, V. R., Loomis, L. D., Michael, N. L., Nara, P. L., and Birx, D. L. (1995) Differential role of V3-specific antibodies in neutralization assays involving primary and laboratory-adapted isolates of HIV type 1. AIDS Res. Hum. Retrovir. 11, 1379–1391.PubMedCrossRefGoogle Scholar
  6. 6.
    Moore, J. P., Cao, Y., Qing, L., Sattentau, Q. J., Pyati, J., Koduri, R., et al. (1995) Primary isolates of human immunodeficiency virus type 1 are relatively resistant to neutralization by monoclonal antibodies to gpl20, and their neutralization is not predicted by studies with monomeric gpl20. J. Virol. 69, 101–109.PubMedGoogle Scholar
  7. 7.
    Moore, J. P. and Sodroski, J. (1996) Antibody cross-competition analysis of the human immunodeficiency virus type 1 gpl20 exterior envelope glycoprotein. J. Virol. 70, 1863–1872.PubMedGoogle Scholar
  8. 8.
    Sattentau, Q. J. and J. P. Moore. (1995) Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gpl20 oligomer. J. Exp. Med. 182, 185–196.PubMedCrossRefGoogle Scholar
  9. 9.
    Gorse, G. J., Frey, S. E., Newman, F. K., and Belshe, R. B. (1992) Detection of binding antibodies to native and recombinant human immunodeficiency virus type 1 envelope glycoproteins following recombinant gpl60 immunization measured by flow cytometry and enzyme immunoassays. The AIDS Vaccine Clinical Trials Network. J. Clin. Microbiol. 30, 2606–2612.PubMedGoogle Scholar
  10. 10.
    Gorse, G. J., Frey, S. E., Patel, G., Newman, F. K., and Belshe, R. B. (1994) Vaccine-induced antibodies to native and recombinant human immunodeficiency virus type 1 envelope glycoproteins. NIAID AIDS Vaccine Clinical Trials Network. Vaccine 12, 912–918.PubMedCrossRefGoogle Scholar
  11. 11.
    VanCott, T. C., Bethke, F. R., Burke, D. S., Redfield, R. R., and Birx, D. L. (1995) Lack of induction of antibodies specific for conserved, discontinuous epitopes of HIV-1 envelope glycoprotein by candidate AIDS vaccines. J. Immunol. 155, 4100–4110.PubMedGoogle Scholar
  12. 12.
    Sattar, S. A. and Springthorpe, V. S. (1991) Survival and disinfectant inactivation of the human immunodeficiency virus: a critical review. Rev. Infect. Dis. 13, 430–447.PubMedGoogle Scholar

Copyright information

© Humana Press Inc., Totowa, NJ 1999

Authors and Affiliations

  • Thomas C. VanCott
    • 1
  • Paul L. Hallberg
    • 2
  1. 1.Henry M. Jackson FoundationRockville
  2. 2.Immunology Vaccine CenterThe University of Alabama at BirminghamBirmingham

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