Peanut allergen

Peanut Allergen checker [Peanut] Oriental Yeast Co., Ltd. Agglutinin precursor gene 95... 

Other applications involve detection of adulteration of dairy products with soy, pea, and wheat proteins (Haasnoot et al., 2001), presence of asrcasein in milk (the detection threshold for this protein was 0.87pg/mL) (Muller-Renaud et al., 2005), [3-casein in milk and cheese (Muller-Renard et al., 2004), and detection of peanut allergenic proteins (the detection threshold for this protein was 0.7 pg/mL) (Mohammed et al., 2001). 

In this BN rat model also various purified weak-, strong- or nonallergenic proteins, based on human experience, have been tested in order to study the relative allergenicity of the selected proteins. In these BN rat studies, 2S albumin purified from Brazil nut (Ber el), a peanut allergen (Ara h 1) purified from peanut, shrimp tropomyosin (Pen al), beef tropomyosin (nonallergenic), and patatin (Sol tl) purified from potatoes were used. These purified proteins were tested in the BN rat model as it was done for OVA using daily gavage with 1 mg of each of the test proteins for 42... 

Li, X.M., Serebrisky, D., Lee, S.J. et al. 2000. A murine model of peanut anaphylaxis T- and B-cell responses to a major peanut allergen mimic human responses. J Allergy Clin Immunol 106 150-158. 

Barre, A., Borges, J.R, Culerrier, R., and Rouge, R 2005. Homology modelling of the major peanut allergen Ara h 2 and surface mapping of IgE-binding epitopes. Immunol Lett 100(2) 153-158. 

Koppelman, S.J., Bruijnzeel-Koomen, C.A., Hessing, M., and de Jongh, H.H. 1999. Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties. J Biol Chem 274(8) 4770-4777. 

Sen, M., Kopper, R., Pons, L., Abraham, E.C., Burks, A.W., and Bannon, G.A. 2002. Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes. J Immunol 169(2) 882-887. 

Shreffler, W.G., Lencer, D.A., Bardina, L., Sampson, H.A. 2005. IgE and IgG4 epitope mapping by microarray immunoassay reveals the diversity of immune response to the peanut allergen, Ara h 2. J Allergy Clin Immunol 116(4) 893—899. 

Recently, Astier and coworkers used purified recombinant peanut allergens rAra h 1, rAra h 2, and rAra h 3 in SPTs and compared the performance of single recombinant allergens to the natural total extract (Astier et al. 2006). The application of these recombinant peanut allergens proved to be a safe method, and reactivity toward individual allergens could be correlated with symptom severity. Either cosensitization to rAra h 1 and rAra h 2 or sensitization to rAra h 3 was predictive of more severe reactions (Astier et al. 2006). 

Peptides that present allergen-specific T-cell epitopes retain the ability to immuno-modulate T-cells, but less an ability to cross-link IgE and activate effectors cells. For example, synthetic peptides-based vaccine derived from major peanut allergen, Ara h 2 composed of thirty 20-mers that overlapped by 15 amino acids (Sicherer and Sampson 2007). Subcutaneous or intranasal administration of the vaccine reduced Ara h 2-specific IgE and plasma histamine release levels as well as anaphylactic symptoms scores in a murine model of peanut anaphylaxis. 

Beardslee, T.A., Zeece, M.G., Sarath, G., and Markwell, J.P. 2000. Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3. Int Arch Allergy Immunol 123 299-307. 

Kolarich, D. and Altmann, F. 2000. N-glycan analysis by matrix-assisted laser desorption/ ionization mass spectrometry of electrophoretically separated nonmammalian proteins Application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1. Anal Biochem 285 64-75. 

Effect of Technological Processes on the Stability of Peanut Allergens.272... 

EFFECT OF TECHNOLOGICAL PROCESSES ON THE STABILITY OF PEANUT ALLERGENS... 

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