Structural aspects of cross-reactivity and its relation to antibody affinity

R. C. Aalberse, I. Kleine Budde, S. O. Stapel, R. van Ree

Research output: Contribution to JournalArticleAcademicpeer-review

21 Citations (Scopus)


In the context of IgE/allergen interactions, affinity is largely determined by the stability of the allergen-IgE complex: a low affinity is usually equated with a rapid dissociation of the complex. Regular solid-phase assays are not well suited for affinity estimates because of multivalency effects, "unstirred layer" effects and "invisible" antibodies. Elution of IgE bound to solid-phase coupled allergen might be a good measure of intrinsic affinity, provided that reassociation of antibodies is prevented by a high concentration of soluble allergen. Allergen-mediated IgE-dependent triggering of a mast cell is presumably a two-step process. During the first step, the allergen is bound to a cell-bound IgE antibody and dragged over the cell surface. The second step is the interaction between this cell-bound allergen and another IgE antibody. The hypothesis is that the affinity requirements for the first step are higher than for the second. The implication is that a mast cell can be triggered by a single high-affinity antibody in combination with one or more low-affinity antibodies
Original languageEnglish
Pages (from-to)27-29
Issue numberSuppl. 67
Publication statusPublished - 2001

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