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Biophys J, May 1999, p. 2421-2431, Vol. 76, No. 5

Quantifying Aggregation of IgE-Fcepsilon RI by Multivalent Antigen

William S. Hlavacek,* Alan S. Perelson,* Bernhard Sulzer,* Jennifer Bold,# Jodi Paar,# Wendy Gorman,§ and Richard G. Posner#

 *Theoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, New Mexico 87545 and the Departments of  #Chemistry and  §Biology, Northern Arizona University, Flagstaff, Arizona 86011 USA

Aggregation of cell surface receptors by multivalent ligand can trigger a variety of cellular responses. A well-studied receptor that responds to aggregation is the high affinity receptor for IgE (Fcepsilon RI), which is responsible for initiating allergic reactions. To quantify antigen-induced aggregation of IgE-Fcepsilon RI complexes, we have developed a method based on multiparameter flow cytometry to monitor both occupancy of surface IgE combining sites and association of antigen with the cell surface. The number of bound IgE combining sites in excess of the number of bound antigens, the number of bridges between receptors, provides a quantitative measure of IgE-Fcepsilon RI aggregation. We demonstrate our method by using it to study the equilibrium binding of a haptenated fluorescent protein, 2,4-dinitrophenol-coupled B-phycoerythrin (DNP25-PE), to fluorescein isothiocyanate-labeled anti-DNP IgE on the surface of rat basophilic leukemia cells. The results, which we analyze with the aid of a mathematical model, indicate how IgE-Fcepsilon RI aggregation depends on the total concentrations of DNP25-PE and surface IgE. As expected, we find that maximal aggregation occurs at an optimal antigen concentration. We also find that aggregation varies qualitatively with the total concentration of surface IgE as predicted by an earlier theoretical analysis.

Biophys J, May 1999, p. 2421-2431, Vol. 76, No. 5
© 1999 by the Biophysical Society   0006-3495/99/05/2421/11  $2.00


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