Identification of IgE-binding peptides in hen egg ovalbumin digested in vitro with human and simulated gastroduodenal fluids
The digestibility of the major egg allergen ovalbumin (OVA, Gal d 2) with human and simulated digestive fluids was assessed. Degradation of OVA was faster when treated with human fluids, particularly following duodenal digestion, leading to gastrointestinal digests with lower IgE binding. Gastric digestion with both systems yielded 52 identical cleavage sites and a similar peptide pattern with 47 peptides in common. Subsequent duodenal digestion showed that the human fluid released fewer and shorter peptides. Several high-frequency IgE-binding epitopes were detected among the fragments of molecular mass lower than 3 kDa identified in the digests: OVA (141-154) and OVA (164-176) in the gastrointestinal digests produced with human fluids; and OVA (125-134), OVA (159-172), OVA (141-154), OVA (188-198), OVA (326-336), and OVA (370-385) in the gastrointestinal digests produced with simulated fluids. The high binding frequency of the fragment OVA (370-385), which reacted with 80% of the sera from allergic patients used, was noteworthy. © 2013 American Chemical Society.
| Main Authors: | , , , |
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| Other Authors: | |
| Format: | artículo biblioteca |
| Published: |
American Chemical Society
2014
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| Subjects: | Epitope, IgE, Human digestive fluids, In vitro digestion, Ovalbumin, Egg allergy, |
| Online Access: | http://hdl.handle.net/10261/100047 http://dx.doi.org/10.13039/501100003339 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100003329 |
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