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The effect of digestion and pH on the allergenicity of kiwifruit proteins

The effect of digestion and pH on the allergenicity of kiwifruit proteins
The effect of digestion and pH on the allergenicity of kiwifruit proteins
It is suggested that patients with oral allergy syndrome (OAS) respond to pepsin-sensitive allergens, and systemic reactors identify pepsin-resistant allergens. We sought to assess the digestibility of kiwifruit proteins in simulated gastric fluid (SGF), and to compare the immunogenicity of the digests in patients with isolated oral and systemic reactions to kiwifruit. In addition, the effect of pH on digestibility of kiwifruit proteins was investigated. The in vitro resistance of kiwifruit proteins to digestion was determined using SGF. G-immunoglobulin (IgE) binding to digested proteins was investigated by Western blotting using sera from children and adults (aged 5-72 yr) with systemic reactions and patients with isolated oral symptoms. To determine whether pH conditions influence digestion of kiwifruit extracts, digestion at pHs 1.5-7 were compared by SDS-PAGE. Patients with systemic reactions showed IgE binding to digestion-resistant allergens, but patients with oral symptoms reacted only to digestion-labile allergens. An increase in pH from 1.5 to 2.5 significantly reduced pepsin breakdown of kiwifruit allergens. Immunoreactive digested protein fragments were detectable by immunoblot but not Coomassie stain. This study confirms a difference in the lability of food allergens recognized by patients with systemic reactions and those with OAS. Pepsin digestion of kiwifruit proteins was impaired by hypoacidic conditions suggesting that patients with hypoacidic gastric conditions are at increased risk of systemic absorption of allergens. The data indicate that commonly used methods for predicting allergenicity of novel proteins using Coomassie stains may be flawed.
0905-6157
392-398
Lucas, Jane S.A.
5cb3546c-87b2-4e59-af48-402076e25313
Cochrane, Stella A.
54225f81-3763-42c6-809f-f16b26e6b6db
Warner, John O.
50630e99-8486-4859-ade3-cd2c79c5a153
Hourihane, Jonathan O'.B.
25de726c-3e91-4fc2-9414-e3974bb22daf
Lucas, Jane S.A.
5cb3546c-87b2-4e59-af48-402076e25313
Cochrane, Stella A.
54225f81-3763-42c6-809f-f16b26e6b6db
Warner, John O.
50630e99-8486-4859-ade3-cd2c79c5a153
Hourihane, Jonathan O'.B.
25de726c-3e91-4fc2-9414-e3974bb22daf

Lucas, Jane S.A., Cochrane, Stella A., Warner, John O. and Hourihane, Jonathan O'.B. (2008) The effect of digestion and pH on the allergenicity of kiwifruit proteins. Pediatric Allergy and Immunology, 19 (5), 392-398. (doi:10.1111/j.1399-3038.2007.00678.x). (PMID:18086217)

Record type: Article

Abstract

It is suggested that patients with oral allergy syndrome (OAS) respond to pepsin-sensitive allergens, and systemic reactors identify pepsin-resistant allergens. We sought to assess the digestibility of kiwifruit proteins in simulated gastric fluid (SGF), and to compare the immunogenicity of the digests in patients with isolated oral and systemic reactions to kiwifruit. In addition, the effect of pH on digestibility of kiwifruit proteins was investigated. The in vitro resistance of kiwifruit proteins to digestion was determined using SGF. G-immunoglobulin (IgE) binding to digested proteins was investigated by Western blotting using sera from children and adults (aged 5-72 yr) with systemic reactions and patients with isolated oral symptoms. To determine whether pH conditions influence digestion of kiwifruit extracts, digestion at pHs 1.5-7 were compared by SDS-PAGE. Patients with systemic reactions showed IgE binding to digestion-resistant allergens, but patients with oral symptoms reacted only to digestion-labile allergens. An increase in pH from 1.5 to 2.5 significantly reduced pepsin breakdown of kiwifruit allergens. Immunoreactive digested protein fragments were detectable by immunoblot but not Coomassie stain. This study confirms a difference in the lability of food allergens recognized by patients with systemic reactions and those with OAS. Pepsin digestion of kiwifruit proteins was impaired by hypoacidic conditions suggesting that patients with hypoacidic gastric conditions are at increased risk of systemic absorption of allergens. The data indicate that commonly used methods for predicting allergenicity of novel proteins using Coomassie stains may be flawed.

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Published date: August 2008

Identifiers

Local EPrints ID: 59368
URI: http://eprints.soton.ac.uk/id/eprint/59368
ISSN: 0905-6157
PURE UUID: ccef65d2-67a1-41d8-a0e9-6987e5f72fb4
ORCID for Jane S.A. Lucas: ORCID iD orcid.org/0000-0001-8701-9975

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Date deposited: 02 Sep 2008
Last modified: 16 Mar 2024 03:25

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Contributors

Author: Jane S.A. Lucas ORCID iD
Author: Stella A. Cochrane
Author: John O. Warner
Author: Jonathan O'.B. Hourihane

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