Inter-laboratory comparisons of assessment of the allergenic potential of proteins in mice

✍ Scribed by C. Herouet-Guicheney; H. Aldemir; R. Bars; D. de Barbeyrac; P. Kennel; D. Rouquié; B. U. Stahl; I. Kimber; R. J. Dearman

• Publisher: John Wiley and Sons
• Year: 2009
• Tongue: English
• Weight: 400 KB
• Volume: 29
• Category: Article
• ISSN: 0260-437X
• DOI: 10.1002/jat.1391

✦ Synopsis

Abstract

Assessment of the potential allergenicity of novel proteins, including those expressed in genetically modified plants, is an important issue. In previous studies, we have shown that the IgE measurement induced by systemic exposure of BALB/c mice to a range of proteins correlates broadly with what is known of their allergenic potential in humans. The approach used a homologous passive cutaneous anaphylaxis (PCA) assay that reflects IgE‐dependent biological activity and is of sufficient sensitivity to detect IgE production in the absence of adjuvant. In previous studies, the immunization phase was conducted independently in two separate facilities, and the subsequent analytical work (PCA) conducted in a single facility. The purpose here was to further evaluate the transferability of this approach. To this end, BALB/c mice were exposed to a range of doses of peanut agglutinin or ovalbumin, allergenic proteins of peanut and hen's egg, respectively, in two independent laboratories. Serial doubling dilutions of serum pooled for each treatment group were analyzed for specific IgE. At higher doses of allergen very similar, or identical, IgE titers were achieved in both laboratories, although at lower doses, responses were somewhat more variable. These data demonstrate that, although technically demanding, the measurement of protein allergen‐induced IgE antibody production in mice using PCA is relatively robust and is transferable and reproducible between laboratories. This approach may provide a useful tool for the safety assessment of novel proteins and suggests that continued evaluation of the approach with a wider range of protein allergens and non‐sensitising proteins is justified. Copyright © 2008 John Wiley & Sons, Ltd.