Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 1992 Aug;63(2):563–568. doi: 10.1016/S0006-3495(92)81610-7

Dimerization kinetics of the IgE-class antibodies by divalent haptens. II. The interactions between intact IgE and haptens.

R Schweitzer-Stenner 1, A Licht 1, I Pecht 1
PMCID: PMC1262178  PMID: 1420898

Abstract

Interactions between a monoclonal, DNP-specific IgE molecules (hybridoma A2) and divalent DNP-haptens in solution cause aggregation of the former predominantly into closed rings of two IgE and two divalent haptens (Schweitzer-Stenner, R., A. Licht, I. Lüscher, and I. Pecht. 1987. Biochemistry. 26:3602-3612). The time course of this process was now investigated by titrating the A2-IgE with divalent DNP-haptens having long and rigid oligoproline spacers (di(N epsilon-2,4-dinitrophenyl)-6-amino-hexanoate-aspartyl-(prolyl)n-L-ly- syl; n = 24, 27, 33). Binding was expressed in quenching of the IgE intrinsic tryptophan emission. As shown in the preceding paper, hapten addition to the IgE-A2 at rates faster than a distinct threshold value led to nonequilibrium titrations (NETs) from which kinetic processes slower than 2 s-1 can be resolved. Analysis of these titrations shows that the dimeric rings open at rates of approximately 10(-2) s-1, independent of the divalent hapten's spacer length. The ring closure rate, however, decreases with spacer length. The latter observation was qualitatively rationalized in terms of the diffusion process of a Gaussian chain which relates the ring closure rate constant to the expectation value for the distance between the free ends of the respective open chain.

Full text

PDF
563

Selected References

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

  1. Archer B. G., Krakauer H. Thermodynamics of antibody-antigen reactions. 2. The binding of bivalent synthetic random coil antigens to antibodies having different antigen precipitating properties. Biochemistry. 1977 Feb 22;16(4):618–627. doi: 10.1021/bi00623a011. [DOI] [PubMed] [Google Scholar]
  2. Balakrishnan K., Hsu F. J., Cooper A. D., McConnell H. M. Lipid hapten containing membrane targets can trigger specific immunoglobulin E-dependent degranulation of rat basophil leukemia cells. J Biol Chem. 1982 Jun 10;257(11):6427–6433. [PubMed] [Google Scholar]
  3. Barsumian E. L., Isersky C., Petrino M. G., Siraganian R. P. IgE-induced histamine release from rat basophilic leukemia cell lines: isolation of releasing and nonreleasing clones. Eur J Immunol. 1981 Apr;11(4):317–323. doi: 10.1002/eji.1830110410. [DOI] [PubMed] [Google Scholar]
  4. DeLisi C. The biophysics of ligand-receptor interactions. Q Rev Biophys. 1980 May;13(2):201–230. doi: 10.1017/s0033583500001657. [DOI] [PubMed] [Google Scholar]
  5. Dembo M., Goldstein B. Theory of equilibrium binding of symmetric bivalent haptens to cell surface antibody: application to histamine release from basophils. J Immunol. 1978 Jul;121(1):345–353. [PubMed] [Google Scholar]
  6. Goldstein B., Posner R. G., Torney D. C., Erickson J., Holowka D., Baird B. Competition between solution and cell surface receptors for ligand. Dissociation of hapten bound to surface antibody in the presence of solution antibody. Biophys J. 1989 Nov;56(5):955–966. doi: 10.1016/S0006-3495(89)82741-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ishizaka T., Ishizaka K. Cell surface IgE on human basophil granulocytes. Ann N Y Acad Sci. 1975 Jun 30;254:462–475. doi: 10.1111/j.1749-6632.1975.tb29194.x. [DOI] [PubMed] [Google Scholar]
  8. Kane P., Erickson J., Fewtrell C., Baird B., Holowka D. Cross-linking of IgE-receptor complexes at the cell surface: synthesis and characterization of a long bivalent hapten that is capable of triggering mast cells and rat basophilic leukemia cells. Mol Immunol. 1986 Jul;23(7):783–790. doi: 10.1016/0161-5890(86)90090-8. [DOI] [PubMed] [Google Scholar]
  9. Ortega E., Schweitzer-Stenner R., Pecht I. Kinetics of ligand binding to the type 1 Fc epsilon receptor on mast cells. Biochemistry. 1991 Apr 9;30(14):3473–3483. doi: 10.1021/bi00228a018. [DOI] [PubMed] [Google Scholar]
  10. Ortega E., Schweitzer-Stenner R., Pecht I. Possible orientational constraints determine secretory signals induced by aggregation of IgE receptors on mast cells. EMBO J. 1988 Dec 20;7(13):4101–4109. doi: 10.1002/j.1460-2075.1988.tb03304.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Posner R. G., Erickson J. W., Holowka D., Baird B., Goldstein B. Dissociation kinetics of bivalent ligand-immunoglobulin E aggregates in solution. Biochemistry. 1991 Mar 5;30(9):2348–2356. doi: 10.1021/bi00223a008. [DOI] [PubMed] [Google Scholar]
  12. Rudolph A. K., Burrows P. D., Wabl M. R. Thirteen hybridomas secreting hapten-specific immunoglobulin E from mice with Iga or Igb heavy chain haplotype. Eur J Immunol. 1981 Jun;11(6):527–529. doi: 10.1002/eji.1830110617. [DOI] [PubMed] [Google Scholar]
  13. Schumaker V. N., Seegan G. W., Smith C. A., Ma S. K., Rodwell J. D., Schumaker M. F. The free energy of angular position of the Fab arms of IgG antibody. Mol Immunol. 1980 Mar;17(3):413–423. doi: 10.1016/0161-5890(80)90063-2. [DOI] [PubMed] [Google Scholar]
  14. Schweitzer-Stenner R., Licht A., Lüscher I., Pecht I. Oligomerization and ring closure of immunoglobulin E class antibodies by divalent haptens. Biochemistry. 1987 Jun 16;26(12):3602–3612. doi: 10.1021/bi00386a053. [DOI] [PubMed] [Google Scholar]
  15. Segal D. M., Taurog J. D., Metzger H. Dimeric immunoglobulin E serves as a unit signal for mast cell degranulation. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2993–2997. doi: 10.1073/pnas.74.7.2993. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES