Serum IgE cross‐reactivity between fish and chicken meats in dogs

Abstract

Background In humans, a cross‐reactive clinical allergy has been reported between three chicken and fish meat proteins: beta‐enolase, aldolase A and parvalbumin. Objective To evaluate if IgE cross‐reactivity between chicken and fish also existed in the dog. Animals Sera from dogs with suspected allergic skin disease and with IgE against chicken and fish. Methods and materials Sera were analysed by ELISA and immunoblotting with chicken, white fish (haddock and cod) and salmon extracts. Reciprocal inhibition ELISAs and inhibition immunoblots were then performed. Protein sequencing of bands identified on multiple extracts was determined by mass spectrometry. Results Out of 53 archived canine sera tested by ELISA against chicken, white fish or salmon, 15 (28%), 12 (23%) and 26 (49%), respectively, had elevated IgE against one, two or all three of these extracts. Seven of the triple‐reactive sera were subjected to reciprocal inhibition ELISAs. A >50% inhibition was found between chicken–fish, chicken–salmon and fish–salmon in seven, four and five of seven dogs, respectively. Immunoblotting identified multiple IgE‐binding proteins of identical molecular weights in the three extracts; these were partially to fully cross‐reactive by inhibition immunoblotting. Mass spectrometry identified nine cross‐reactive proteins as: pyruvate kinase, creatine kinase, alpha‐actin, glyceraldehyde‐3‐phosphate dehydrogenase, beta‐enolase, aldolase, malate dehydrogenase, lactate dehydrogenase and triose‐phosphate isomerase 1. All of these have been reported previously as fish, shellfish and/or chicken allergens for humans. Conclusions and clinical importance Whether any of these newly identified IgE cross‐reactive chicken–fish allergens is the cause of clinical allergy needs to be determined in dogs reacting to at least two of these common food sources.

Serum IgE and IgG responses to dietary antigens in dogs with and without cutaneous adverse food reactions

“…Although the identity of these bands remains unknown, the sizes of the epitopes corresponded well with proteins previously demonstrated to bind canine serum IgE. 10,11,13 Extensive binding of canine IgG to almost all of the proteins in the test extracts was also demonstrated, regardless of prior reported dietary exposure to these foods. This finding suggests that prior exposure to foods not reported in dietary histories may be much more frequent than expected.…”

“…In conclusion, several IgE‐binding epitopes were identified in beef, milk and chicken extracts. Although the identity of these bands remains unknown, the sizes of the epitopes corresponded well with proteins previously demonstrated to bind canine serum IgE . Extensive binding of canine IgG to almost all of the proteins in the test extracts was also demonstrated, regardless of prior reported dietary exposure to these foods.…”

“…Other, more likely possibilities include aldolase A (40 kDa), alpha 1 actin (42 kDa) or creatine kinase type M (43 kDa), all of which have previously been identified as canine IgE-binding proteins. 13 Beef (and, to a lesser extent, milk) extract yielded two differentially identified bands. A 52 kDa band in beef was identified twice as frequently in FR as in NFR sera.…”

“…These studies have identified as putative food allergens in dogs: pyruvate kinase M 1/2, Enolase 3, M-type creatine kinase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase a and triose phosphate isomerase 1 in chicken; bconglycinin in soybean; phosphoglucomutase, the bovine IgG heavy chain, and (to date unidentified) bands of 42, 37, 33, 31 and 27 kDa in milk; ovomucoid and ovalbumin in egg; and the IgG heavy chain and bovine serum albumin in beef. [9][10][11][12][13] Many of these allergens have been identified using archived sera (or pools of archived sera) preselected for IgE reactivity against the food source of interest, often with no clinical information available. Furthermore, this reactivity has generally been determined relative either to healthy dogs, or to dogs pre-selected as nonreactive against the food sources.…”

Co‐reactivity between related and unrelated environmental allergens in equine allergen‐specific IgE serology testing in the UK

“…Further work using cross‐inhibition ELISAs is required to establish whether this co‐reactivity was due to co‐sensitization (separate IgE‐binding epitopes) or to antigenic cross‐reactivity (shared IgE‐binding epitopes) . Any cross‐reacting proteins can then subsequently be identified by Western blotting and mass spectrometry . Improving knowledge of cross‐reactivity between allergens is of clinical importance for optimizing strategies for allergen avoidance (where practical) and/or ASIT.…”