Vertebrate Tropomyosin as an Allergen

Peixoto, Sara; Monteiro, Tânia; Carvalho, Marisa; Santos, Maria Conceição Pereira; Matos, C; Bartolomé, B; Labrador‐Horrillo, Moisés; Quaresma, Márcia

doi:10.18176/jiaci.0206

Cited by 18 publications

(24 citation statements)

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“…Tropomyosin is a major allergen that is the cause of many forms of crustacean allergy [33] as well as mite allergy [34] in humans. Although comparison of the tropomyosin protein sequence revealed a low sequence similarity between cod and shrimp (Table S2), fish-shrimp cross-reactivity was previously reported in humans [35,36]. Additionally, mite-crustacean cross-reactivity was widely reported in humans, and the tropomyosin sequence similarity between the two species is over 90% [37].…”

Section: Discussionmentioning

confidence: 99%

“…The results of the current study also revealed enolase is a potential allergen associated with canine fish allergy (Figure 3 and Table 1). Enolase was recently defined as a fish allergen that exhibited cross-reactivity to chicken in humans and dogs [36,39]. Numerous fish proteins, other than those purified proteins that are recognized as critical allergenic components in humans, have been registered in the International Union of Immunological Societies allergen database [40].…”

Section: Discussionmentioning

confidence: 99%

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IgE reactivity to fish allergens in Pacific cod (Gadus macrocephalus) in atopic dogs

Imanishi

Uchiyama

Mizukami

et al. 2020

Preprint

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Background: IgE reactivity to fish allergens in atopic dogs, which are used as models for food allergy, has not been elucidated to date. We investigated IgE reactivity to crude extracts and purified Pacific cod (Gadus macrocephalus) allergens in atopic dogs to identify the allergenic proteins of cod.Methods: Specific IgE to crude cod extracts in the sera of 179 atopic dogs, including 27 dogs with cod allergy, were measured using enzyme-linked immunosorbent assay (ELISA). The allergens of crude cod extracts were analyzed by ELISA, immunoblotting, and liquid chromatography-tandem mass spectrometry (LC-MS/MS). IgE reactivity to parvalbumin, collagen, and tropomyosin was evaluated using the sera of atopic dogs that were positive for specific IgE to crude cod extracts.Results: Specific IgE to crude cod extracts were present in 36 (20%) of the 179 atopic dogs and 12 (44%) of the 27 dogs with cod allergy. In allergen component analysis, IgE reactivity to tropomyosin and enolase was observed in the sera of dogs with cod allergy. Among the 36 dogs with IgE reactivity to crude cod extracts, 9 (25%), 14 (39%), and 18 (50%) dogs had specific IgE to parvalbumin, collagen, and tropomyosin, respectively.Conclusions: The dogs exhibited IgE reactivity to the cod allergens which observed in humans, providing support for the use of atopic dogs with fish allergy as a model for fish allergy in humans.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

IgE reactivity to fish allergens in Pacific cod (Gadus macrocephalus) in atopic dogs

Imanishi

Uchiyama

Mizukami

et al. 2020

Preprint

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“…Identification of appropriate calibrators and predictive assays would allow for the future assessment of allergenicity of novel food proteins. Indeed, invertebrate TM is a known food allergen while only few studies relate vertebrate TM to clinical food allergy (eg in fish) …”

Section: Discussionmentioning

confidence: 99%

Homologous tropomyosins from vertebrate and invertebrate: Recombinant calibrator proteins in functional biological assays for tropomyosin allergenicity assessment of novel animal foods

Klueber

Costa

Randow

et al. 2019

Clin Experimental Allergy

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Background: Novel foods may provide new protein sources for a growing world population but entail risks of unexpected food-allergic reactions. No guidance on allergenicity assessment of novel foods exists, while for genetically modified (GM) crops it includes comparison of sequence identity with known allergens, digestibility tests and IgE serum screening.Objective: As a proof of concept, to evaluate non-/allergenic tropomyosins (TMs) regarding their potential as new calibrator proteins in functional biological in vitro assays for the semi-quantitative allergy risk assessment of novel TM-containing animal foods with mealworm TM as an example. Methods:Purified TMs (shrimp, Penaeus monodon; chicken Gallus gallus; E coli overexpression) were compared by protein sequencing, circular dichroism analysis and in vitro digestion. IgE binding was quantified using shrimp-allergic patients' sera (ELISA).Biological activities were investigated (skin testing; titrated basophil activation tests, BAT), compared to titrated biological mediator release using humanized rat basophil leukaemia (RBL) cells.Results: Shrimp and chicken TMs showed high sequence homology, both alpha-helical structures and thermal stability. Shrimp TM was stable during in vitro gastric digestion, chicken TM degraded quickly. Both TMs bound specific IgE from shrimp-allergic patients (significantly higher for shrimp TM), whereas skin reactivity was mostly positive with only shrimp TM. BAT and RBL cell assays were positive with shrimp and chicken TM, although at up to 100-to 1000-times lower allergen concentrations for shrimp than chicken TM. In RBL cell assays using both TM as calibrators, an activation of effector cells by mealworm TM similar to that by shrimp TM confirmed the already reported high allergenic potency of mealworm TM as a novel protein source.Conclusions & clinical relevance: According to current GM crops' allergenicity assessment, non-allergenic chicken TM could falsely be considered an allergen on a weight-of-evidence approach. However, calibrating allergenic potency in functional BAT and RBL cell assays with clinically validated TMs allowed for semi-quantitative discrimination of novel food protein's allergenicity. With TM calibration as a proof of concept, similar systems of homologous protein might be developed to scale on an axis of allergenicity. K E Y W O R D Sallergenicity assessment, basophil activation test, chicken, rat basophil leukaemia cell mediator release, shrimp, shrimp allergy, tropomyosin

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“…The homology between invertebrate tropomyosin and fish tropomyosin is only 57%, which, theoretically, is not sufficient to lead to clinical cross-reactivity [39]. However, Peixoto et al [41] described a child suspected of clinical cross-reactivity between fish and shrimp tropomyosin.…”

Section: Other Allergensmentioning

confidence: 99%

What Do We Know About Fish Allergy at the End of the Decade?

Kourani¹,

Corazza²,

Michel³

et al. 2019

J Investig Allergol Clin Immunol

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Fish allergy is one of the most common food allergies. It is usually considered to be IgE-mediated and correlates well with diagnostic tests such as prick tests and/or determination of specific IgE. Avoidance is the recommended treatment and is generally extended to all fish species. However, new clinical presentations have been described. These include non-IgE-mediated disease, monosensitization, and new syndromes that are sometimes associated, surprisingly, with cross-reactivity. Advances in molecular allergy have provided insights into new allergens and have increased our understanding of cross-reactivity. This paper focuses on recent publications providing information for clinicians involved in the management of fish allergy.

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Vertebrate Tropomyosin as an Allergen

Cited by 18 publications

References 0 publications

IgE reactivity to fish allergens in Pacific cod (Gadus macrocephalus) in atopic dogs

IgE reactivity to fish allergens in Pacific cod (Gadus macrocephalus) in atopic dogs

Homologous tropomyosins from vertebrate and invertebrate: Recombinant calibrator proteins in functional biological assays for tropomyosin allergenicity assessment of novel animal foods

What Do We Know About Fish Allergy at the End of the Decade?

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