Plant Food Allergens 2003
DOI: 10.1002/9780470995174.ch8
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Bet v 1‐Homologous Allergens

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Cited by 4 publications
(5 citation statements)
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“…These homologous allergens show a high similarity in primary, secondary and tertiary structure. At the amino acid level, the fruit allergens Mal d 1 and Pru av 1 show 64 -66% sequence identity with Bet v 1, compared to 44% for the homologous vegetable allergens Api g 1 and Dau c 1 [10]. The secondary and tertiary protein structures also exhibit a high degree of similarity, as shown in X-ray crystallization and NMR studies of Bet v 1 and Pru av 1 [11 -13].…”
Section: Introductionmentioning
confidence: 97%
“…These homologous allergens show a high similarity in primary, secondary and tertiary structure. At the amino acid level, the fruit allergens Mal d 1 and Pru av 1 show 64 -66% sequence identity with Bet v 1, compared to 44% for the homologous vegetable allergens Api g 1 and Dau c 1 [10]. The secondary and tertiary protein structures also exhibit a high degree of similarity, as shown in X-ray crystallization and NMR studies of Bet v 1 and Pru av 1 [11 -13].…”
Section: Introductionmentioning
confidence: 97%
“…In soybean, the Bet v 1 homologue SAM22 allergen consists of ten genes present in a tandem array (Crowell et al 1992;KleineTebbe et al 2002). Fourth, Bet v 1-related genes are expressed in different tissues and under biotic or abiotic stresses (Hoffmann-Sommergruber and Radauer 2004). Several expression studies on apple Mal d 1 genes also showed some differences for individual genes.…”
Section: Mal D 1 Gene Family Organization and Evolutionary Originmentioning
confidence: 99%
“…Recombinant by expressed proteins of these isoallergens and variants identified in this study can be used to assess their allergenicity. (Hoffmann-Sommergruber et al 2004). In soybean, the Bet v 1 homologue SAM22 allergen consists of ten genes present in a tandem array (Crowell et al 1992;KleineTebbe et al 2002).…”
Section: Mal D 1 Gene Family Organization and Evolutionary Originmentioning
confidence: 99%
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“…Mal d 1 and Mal d 4 allergens are heat labile and sensitive to proteolytic degradation, while Mal d 2 and Mal d 3 allergens are resistant to heat and stable to proteolytic degradation. Mal d 1 and the Mal d 2 proteins are the most significant apple allergens inducing IgE-mediated hypersensitivity reaction (Hoffmann-Sommergruber & Radauer, 2004).…”
Section: Introductionmentioning
confidence: 99%