BACKGROUND: The allergens responsible for cashew food allergy have not been well characterized. OBJECTIVES: We initiated a study to clone cDNAs encoding cashew food allergens. METHODS: A cashew cDNA library was screened with human serum for IgE-reactive clones and rabbit IgG anti-cashew extract antisera. Reactive clones were sequenced and expressed, and linear epitopes were identified by means of solid-phase overlapping peptide analysis. Immunoblot inhibition was used to identify the native peptide in cashew extract. RESULTS: Four closely related clones reactive with both human and rabbit antisera were sequenced. Sequence analysis showed that these encode members of the vicilin/sucrose-binding protein family of plant seed storage proteins. Screening of the recombinant protein with sera from 20 patients with cashew allergy and 8 cashew-tolerant patients with allergies to other tree nuts showed that 50% and 25% of sera from patients with cashew allergy and cashew-tolerant subjects, respectively, bound the recombinant protein. The corresponding native allergen protein, designated Ana o 1, was located at approximately 50 kd. Epitope mapping revealed 11 linear IgE-binding epitopes, of which 3 appear to be immunodominant. None of the epitopes were shared in common with those of the peanut vicilin allergen Ara h 1. CONCLUSION: Ana o 1, a vicilin-like protein, is a major food allergen in cashews. Cashew and peanut vicilins do not share linear epitopes.
BACKGROUND: The allergens responsible for cashewfood allergy have not been well characterized. OBJECTIVES: We initiated a study to clone cDNAs encoding cashewfood allergens. METHODS: A cashew cDNA library was screened with human serum for IgE-reactive clones and rabbit IgG anti-cashew extract antisera. Reactive clones were sequenced and expressed, and linear epitopes were identified by means of solid-phase overlapping peptide analysis. Immunoblot inhibition was used to identify the native peptide in cashew extract. RESULTS: Four closely related clones reactive with both human and rabbit antisera were sequenced. Sequence analysis showed that these encode members of the vicilin/sucrose-binding protein family of plant seed storage proteins. Screening of the recombinant protein with sera from 20 patients with cashewallergy and 8 cashew-tolerant patients with allergies to other tree nuts showed that 50% and 25% of sera from patients with cashewallergy and cashew-tolerant subjects, respectively, bound the recombinant protein. The corresponding native allergen protein, designated Ana o 1, was located at approximately 50 kd. Epitope mapping revealed 11 linear IgE-binding epitopes, of which 3 appear to be immunodominant. None of the epitopes were shared in common with those of the peanut vicilin allergen Ara h 1. CONCLUSION: Ana o 1, a vicilin-like protein, is a major food allergen in cashews. Cashew and peanut vicilins do not share linear epitopes.
Authors: Alexander C Y Foo; Jacqueline B Nesbit; Stephen A Y Gipson; Hsiaopo Cheng; Pierre Bushel; Eugene F DeRose; Catherine H Schein; Suzanne S Teuber; Barry K Hurlburt; Soheila J Maleki; Geoffrey A Mueller Journal: J Agric Food Chem Date: 2022-02-09 Impact factor: 5.279
Authors: L D Archila; I-T Chow; J W McGinty; A Renand; D Jeong; D Robinson; M L Farrington; W W Kwok Journal: Clin Exp Allergy Date: 2016-06 Impact factor: 5.018
Authors: Iris Lauer; Kay Foetisch; Daniel Kolarich; Barbara K Ballmer-Weber; Amedeo Conti; Friedrich Altmann; Stefan Vieths; Stephan Scheurer Journal: Biochem J Date: 2004-10-15 Impact factor: 3.857
Authors: Christian Lupinek; Eva Wollmann; Alexandra Baar; Srinita Banerjee; Heimo Breiteneder; Barbara M Broecker; Merima Bublin; Mirela Curin; Sabine Flicker; Tetiana Garmatiuk; Heidrun Hochwallner; Irene Mittermann; Sandra Pahr; Yvonne Resch; Kenneth H Roux; Bharani Srinivasan; Sebastian Stentzel; Susanne Vrtala; Leanna N Willison; Magnus Wickman; Karin C Lødrup-Carlsen; Josep Maria Antó; Jean Bousquet; Claus Bachert; Daniel Ebner; Thomas Schlederer; Christian Harwanegg; Rudolf Valenta Journal: Methods Date: 2013-10-22 Impact factor: 3.608