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Evaluation of IgE binding to proteins of hardy (Actinidia arguta), gold (Actinidia chinensis) and green (Actinidia deliciosa) kiwifruits and processed hardy kiwifruit concentrate, using sera of individuals with food allergies to green kiwifruit

Evaluation of IgE binding to proteins of hardy (Actinidia arguta), gold (Actinidia chinensis) and green (Actinidia deliciosa) kiwifruits and processed hardy kiwifruit concentrate, using sera of individuals with food allergies to green kiwifruit
Evaluation of IgE binding to proteins of hardy (Actinidia arguta), gold (Actinidia chinensis) and green (Actinidia deliciosa) kiwifruits and processed hardy kiwifruit concentrate, using sera of individuals with food allergies to green kiwifruit
BACKGROUND: Allergy to green kiwifruit has become common since the fruit was introduced in North America and Europe 30 years ago. Gold kiwifruit, more recently introduced commercially, has been shown to bind IgE from some individuals allergic to green kiwifruit. Hardy kiwifruit is a third species that is now cultivated in North America with potential application as a fresh fruit and in processed foods.

OBJECTIVE: To compare the IgE binding properties of proteins in hardy kiwifruit extract and processed hardy kiwifruit concentrate to each other and to extracts of green and gold kiwifruits to evaluate the potential for allergic cross-reactions.

METHODS: Sera from kiwifruit-allergic subjects and individuals without allergies to kiwifruit were assayed for IgE binding to soluble proteins in green, gold and hardy kiwifruits and heat-processed concentrate from hardy kiwifruit using immunoblots and direct enzyme-linked immunosorbent assay (ELISA).

RESULTS: Marked IgE binding to specific hardy kiwifruit proteins was identified. However, IgE binding to heat-processed hardy kiwifruit concentrate was remarkably lower than to the raw fruit extract.

CONCLUSIONS: These results suggest that some kiwifruit-allergic individuals may suffer allergic cross-reactions if they consume raw hardy kiwifruit. However, heat processing of the hardy kiwifruit alters allergenic protein structure, dramatically reducing in vitro IgE binding. Processing likely reduces the risk of eliciting an allergic response in those with allergies to raw kiwifruit.

Abbreviations: Act c 1, cysteine protease; Act c 2, thaumatin-like protein; DBPCFC, double-blinded, placebo-controlled food challenge; NFDM, non-fat dried milk; PBST, phosphate buffered saline with Tween-20; SPT, skin prick test
kiwi, allergen, ige, cross-reactivity
0278-6915
1100-1107
Chen, Lingyun
ea906c65-504d-4b28-9878-37c813f921d1
Lucas, Jane S.
5cb3546c-87b2-4e59-af48-402076e25313
Hourihane, Jonathan O.
9432101b-1ce1-456c-93a3-56551969ba01
Lindemann, Julianne
e997d8dd-ef86-4d10-90d6-0ffa129f6d50
Taylor, Steve L.
8b0723e6-4626-491e-9bf5-8bd4bc9307c4
Goodman, Richard E.
df086097-b19a-4327-b0f0-b22f4fc8ee29
Chen, Lingyun
ea906c65-504d-4b28-9878-37c813f921d1
Lucas, Jane S.
5cb3546c-87b2-4e59-af48-402076e25313
Hourihane, Jonathan O.
9432101b-1ce1-456c-93a3-56551969ba01
Lindemann, Julianne
e997d8dd-ef86-4d10-90d6-0ffa129f6d50
Taylor, Steve L.
8b0723e6-4626-491e-9bf5-8bd4bc9307c4
Goodman, Richard E.
df086097-b19a-4327-b0f0-b22f4fc8ee29

Chen, Lingyun, Lucas, Jane S., Hourihane, Jonathan O., Lindemann, Julianne, Taylor, Steve L. and Goodman, Richard E. (2006) Evaluation of IgE binding to proteins of hardy (Actinidia arguta), gold (Actinidia chinensis) and green (Actinidia deliciosa) kiwifruits and processed hardy kiwifruit concentrate, using sera of individuals with food allergies to green kiwifruit. Food and Chemical Toxicology, 44 (7), 1100-1107. (doi:10.1016/j.fct.2006.01.005). (PMID:16481086)

Record type: Article

Abstract

BACKGROUND: Allergy to green kiwifruit has become common since the fruit was introduced in North America and Europe 30 years ago. Gold kiwifruit, more recently introduced commercially, has been shown to bind IgE from some individuals allergic to green kiwifruit. Hardy kiwifruit is a third species that is now cultivated in North America with potential application as a fresh fruit and in processed foods.

OBJECTIVE: To compare the IgE binding properties of proteins in hardy kiwifruit extract and processed hardy kiwifruit concentrate to each other and to extracts of green and gold kiwifruits to evaluate the potential for allergic cross-reactions.

METHODS: Sera from kiwifruit-allergic subjects and individuals without allergies to kiwifruit were assayed for IgE binding to soluble proteins in green, gold and hardy kiwifruits and heat-processed concentrate from hardy kiwifruit using immunoblots and direct enzyme-linked immunosorbent assay (ELISA).

RESULTS: Marked IgE binding to specific hardy kiwifruit proteins was identified. However, IgE binding to heat-processed hardy kiwifruit concentrate was remarkably lower than to the raw fruit extract.

CONCLUSIONS: These results suggest that some kiwifruit-allergic individuals may suffer allergic cross-reactions if they consume raw hardy kiwifruit. However, heat processing of the hardy kiwifruit alters allergenic protein structure, dramatically reducing in vitro IgE binding. Processing likely reduces the risk of eliciting an allergic response in those with allergies to raw kiwifruit.

Abbreviations: Act c 1, cysteine protease; Act c 2, thaumatin-like protein; DBPCFC, double-blinded, placebo-controlled food challenge; NFDM, non-fat dried milk; PBST, phosphate buffered saline with Tween-20; SPT, skin prick test

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More information

Published date: July 2006
Keywords: kiwi, allergen, ige, cross-reactivity

Identifiers

Local EPrints ID: 45374
URI: https://eprints.soton.ac.uk/id/eprint/45374
ISSN: 0278-6915
PURE UUID: ec55ee8d-fa78-438b-bcb1-4abbd2a8306c

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Date deposited: 23 Mar 2007
Last modified: 13 Mar 2019 21:05

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