Skip to main content
PMC home page
Immunology logoLink to Immunology
. 1988 Dec;65(4):611–615.

Individuals infected with HIV possess antibodies against IL-2.

K L Bost 1, B H Hahn 1, M S Saag 1, G M Shaw 1, D A Weigent 1, J E Blalock 1
PMCID: PMC1385572  PMID: 2464543

Abstract

Studies are presented here which demonstrate that antibodies reacting with human interleukin-2 (IL-2) are present in the sera of patients infected with the human immunodeficiency virus (HIV). It is likely that these antibodies are present due to a homology between the HIV envelope protein and IL-2. The homologues are six amino acids in length corresponding to the carboxy terminus of gp41, Leu-Glu-Arg-Ile-Leu-Leu (LERILL), and residues 14-19 of secreted IL-2, Leu-Glu-His-Leu-Leu-Leu (LEHLLL). Thus, we questioned whether antibodies made against this HIV envelope peptide would cross-react with IL-2. Not only do a high percentage of the HIV-infected individuals tested here have antibodies against LERILL, but these antibodies cross-react with the IL-2 sequence, LEHLLL. Additional antigenic processing of IL-2 is suggested by the finding that epitopes other than this sixmer are also recognized by antibodies in patients' sera. Thus, these studies suggest a mechanism by which infection with HIV can induce a potentially suppressive autoimmune response. Specifically, antibodies against an HIV envelope peptide cross-react with an epitope in IL-2.

Full text

PDF
613

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bost K. L., Smith E. M., Blalock J. E. Regions of complementarity between the messenger RNAs for epidermal growth factor, transferrin, interleukin-2 and their respective receptors. Biochem Biophys Res Commun. 1985 May 16;128(3):1373–1380. doi: 10.1016/0006-291x(85)91092-7. [DOI] [PubMed] [Google Scholar]
  2. Brandhuber B. J., Boone T., Kenney W. C., McKay D. B. Three-dimensional structure of interleukin-2. Science. 1987 Dec 18;238(4834):1707–1709. doi: 10.1126/science.3500515. [DOI] [PubMed] [Google Scholar]
  3. Gluckman J. C., Klatzmann D., Montagnier L. Lymphadenopathy-associated-virus infection and acquired immunodeficiency syndrome. Annu Rev Immunol. 1986;4:97–117. doi: 10.1146/annurev.iy.04.040186.000525. [DOI] [PubMed] [Google Scholar]
  4. Granelli-Piperno A., Andrus L., Reich E. Antibodies to interleukin 2. Effects on immune responses in vitro and in vivo. J Exp Med. 1984 Sep 1;160(3):738–750. doi: 10.1084/jem.160.3.738. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hahn B. H., Shaw G. M., Taylor M. E., Redfield R. R., Markham P. D., Salahuddin S. Z., Wong-Staal F., Gallo R. C., Parks E. S., Parks W. P. Genetic variation in HTLV-III/LAV over time in patients with AIDS or at risk for AIDS. Science. 1986 Jun 20;232(4757):1548–1553. doi: 10.1126/science.3012778. [DOI] [PubMed] [Google Scholar]
  6. Ju G., Collins L., Kaffka K. L., Tsien W. H., Chizzonite R., Crowl R., Bhatt R., Kilian P. L. Structure-function analysis of human interleukin-2. Identification of amino acid residues required for biological activity. J Biol Chem. 1987 Apr 25;262(12):5723–5731. [PubMed] [Google Scholar]
  7. Ratner L., Haseltine W., Patarca R., Livak K. J., Starcich B., Josephs S. F., Doran E. R., Rafalski J. A., Whitehorn E. A., Baumeister K. Complete nucleotide sequence of the AIDS virus, HTLV-III. Nature. 1985 Jan 24;313(6000):277–284. doi: 10.1038/313277a0. [DOI] [PubMed] [Google Scholar]
  8. Redfield R. R., Wright D. C., Tramont E. C. The Walter Reed staging classification for HTLV-III/LAV infection. N Engl J Med. 1986 Jan 9;314(2):131–132. doi: 10.1056/NEJM198601093140232. [DOI] [PubMed] [Google Scholar]
  9. Reiher W. E., 3rd, Blalock J. E., Brunck T. K. Sequence homology between acquired immunodeficiency syndrome virus envelope protein and interleukin 2. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9188–9192. doi: 10.1073/pnas.83.23.9188. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Smith K. A. Interleukin 2. Annu Rev Immunol. 1984;2:319–333. doi: 10.1146/annurev.iy.02.040184.001535. [DOI] [PubMed] [Google Scholar]
  11. Starcich B. R., Hahn B. H., Shaw G. M., McNeely P. D., Modrow S., Wolf H., Parks E. S., Parks W. P., Josephs S. F., Gallo R. C. Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS. Cell. 1986 Jun 6;45(5):637–648. doi: 10.1016/0092-8674(86)90778-6. [DOI] [PubMed] [Google Scholar]
  12. Taniguchi T., Matsui H., Fujita T., Takaoka C., Kashima N., Yoshimoto R., Hamuro J. Structure and expression of a cloned cDNA for human interleukin-2. Nature. 1983 Mar 24;302(5906):305–310. doi: 10.1038/302305a0. [DOI] [PubMed] [Google Scholar]
  13. Weigent D. A., Hoeprich P. D., Bost K. L., Brunck T. K., Reiher W. E., 3rd, Blalock J. E. The HTLV-III envelope protein contains a hexapeptide homologous to a region of interleukin-2 that binds to the interleukin-2 receptor. Biochem Biophys Res Commun. 1986 Aug 29;139(1):367–374. doi: 10.1016/s0006-291x(86)80123-1. [DOI] [PubMed] [Google Scholar]

Articles from Immunology are provided here courtesy of British Society for Immunology

RESOURCES