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. 2000 May 1;191(9):1555–1567. doi: 10.1084/jem.191.9.1555

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Heterophilic adhesion of IELs (A) and K562-α_Eβ₇ (B) to E-cadherin-Fc mutants. Using adhesion to saturating amounts of E-cadherin-Fc, the mean adhesion to each mutant is expressed relative to adhesion to wild-type E-cadherin-Fc (% cells bound to mutant E-cadherin-Fc/% cells bound to wild-type E-cadherin-Fc × 100). Adhesion to wild-type E-cadherin-Fc is shown as 100%. Adhesion above the saturating dose was chosen to minimize the effect of any errors in quantitation of the fusion protein. Mutation KEG30-32RDT is abbreviated KEG. The loop containing the mutated residues is marked below the lines. Results are shown as the mean ± 1 SD of at least two independent experiments in which each condition was performed in triplicate. A two-sided t test was used to compare the mean value of IEL adhesion to each E-cadherin-Fc mutant with the mean value of IEL adhesion to wild-type E-cadherin-Fc. (A) IEL adhesion to the panel of E-cadherin-Fc mutants. Statistically significant differences are observed for KEG30-32RDT (P ≤ 0.0001), E31A (P ≤ 0.0001), E31D (P ≤ 0.0001), and E89A (P ≤ 0.0001). (B) K562-α_Eβ₇ adhesion to the section of E-cadherin-Fc mutants. Statistically significant differences are observed for N27A (P ≤ 0.0001), K28A (P ≤ 0.0001), K30A (P ≤ 0.0001), KEG30-32RDT (P ≤ 0.0001), E31A (P ≤ 0.0001), E31D (P ≤ 0.0001), N86A (P ≤ 0.0017), and E89A (P ≤ 0.0001).