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HIV Protocols pp 265–271Cite as

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

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Part of the book series: Methods in Molecular Medicine™ ((MIMM,volume 17))

Abstract

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 (1–4). 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 (6–8).

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References

  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.

    PubMed  CAS  Google Scholar 

  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.

    Article  PubMed  CAS  Google Scholar 

  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.

    PubMed  CAS  Google Scholar 

  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.

    Article  PubMed  CAS  Google Scholar 

  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.

    Article  PubMed  CAS  Google Scholar 

  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.

    PubMed  CAS  Google Scholar 

  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.

    PubMed  CAS  Google Scholar 

  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.

    Article  PubMed  CAS  Google Scholar 

  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.

    PubMed  CAS  Google Scholar 

  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.

    Article  PubMed  CAS  Google Scholar 

  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.

    PubMed  CAS  Google Scholar 

  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.

    PubMed  CAS  Google Scholar 

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Author information

Authors and Affiliations

  1. Henry M. Jackson Foundation, Rockville, MD

    Thomas C. VanCott

  2. Immunology Vaccine Center, The University of Alabama at Birmingham, Birmingham, AL

    Paul L. Hallberg

Authors
  1. Thomas C. VanCott
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  2. Paul L. Hallberg
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Editor information

Editors and Affiliations

  1. Walter Reed Army Institute of Research, Rockville, MD

    Nelson L. Michael MD, PhD

  2. Henry M. Jackson Foundation, Rockville, MD

    Jerome H. Kim MD

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© 1999 Humana Press Inc., Totowa, NJ

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VanCott, T.C., Hallberg, P.L. (1999). Analysis of Antibody Interactions with HIV-1 Envelope Expressed on the Surface of Acutely Infected H9 Cells. In: Michael, N.L., Kim, J.H. (eds) HIV Protocols. Methods in Molecular Medicine™, vol 17. Humana Press. https://doi.org/10.1385/0-89603-369-4:265

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  • DOI: https://doi.org/10.1385/0-89603-369-4:265

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-369-6

  • Online ISBN: 978-1-59259-601-0

  • eBook Packages: Springer Protocols

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