Cross-reaction of recombinant termite ( Coptotermes formosanus ) tropomyosin with IgE from cockroach and shrimp allergic individuals

Vargas, Aurora M.; Mahajan, Avanika; Tille, Katherine S.; Wilson, Bridget S.; Mattison, Christopher P.

doi:10.1016/j.anai.2017.12.017

Cited by 7 publications

(5 citation statements)

References 10 publications

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“…Studies have demonstrated that TM is an important allergen in other crustaceans, such as crabs (Cha f 1, Por p 1, Scy p 1) and lobsters (Pan s 1, Hom a 1, Pan s 1), as well as mollusks such as oysters (Cra a 1, Cra g 1, Sac g 1), gastropods (Hal l 1, Hal m 1, Hel as 1), and squid (Tod p 1) (Table 3). In addition to shellfish, it is characterized as a food allergen in herring worm (Ani s 3) [78], common roundworm (Asc l 3), silk moth (Bomb m 3) [79], and Mozambique tilapia (Ore m 4) [80], as an airway allergen in mosquitoes (Aed a 10) [81], cockroaches (Bla g 7, Per a 7) [82,83], mites (Blo t 10, Cho a 10, Der f 10, Der p 10, Lep d 10, Tyr p 10) [84][85][86][87][88][89], and termites (Copt f 7) [81], and as an injection allergen in midges (Chi k 10) [90]. AK is also a widely distributed invertebrate pan-allergen with remarkably conserved sequences and shows cross-reactivity with allergens from crab (Cal b 2, Scy p 2) and oyster (Cra a 2) (Table 3).…”

Section: Cross-reactivity Of Shrimp Allergensmentioning

confidence: 99%

Genomics of Shrimp Allergens and Beyond

Li,

Chu,

Wai

2023

Genes

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Allergy to shellfishes, including mollusks and crustaceans, is a growing health concern worldwide. Crustacean shellfish is one of the “Big Eight” allergens designated by the U.S. Food and Drug Administration and is the major cause of food-induced anaphylaxis. Shrimp is one of the most consumed crustaceans triggering immunoglobulin E (IgE)-mediated allergic reactions. Over the past decades, the allergen repertoire of shrimp has been unveiled based on conventional immunodetection methods. With the availability of genomic data for penaeid shrimp and other technological advancements like transcriptomic approaches, new shrimp allergens have been identified and directed new insights into their expression levels, cross-reactivity, and functional impact. In this review paper, we summarize the current knowledge on shrimp allergens, as well as allergens from other crustaceans and mollusks. Specific emphasis is put on the genomic information of the shrimp allergens, their protein characteristics, and cross-reactivity among shrimp and other organisms.

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Section: Cross-reactivity Of Shrimp Allergensmentioning

confidence: 99%

Genomics of Shrimp Allergens and Beyond

Li,

Chu,

Wai

2023

Genes

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“…In addition, they demonstrated that a recombinant termite tropomyosin cross-reacted with IgE from patients with cockroach and shrimp allergy. 43 Two cases of anaphylaxis due to grasshopper allergy 44 in polysensitized patients to HDM, cockroach, and crustaceans were described. Both patients had a clinical history of urticaria and angioedema after the ingestion of crustaceans and onset of an anaphylactic reaction after the ingestion of chapulines and grasshopper.…”

Section: Tropomyosin and Insectsmentioning

confidence: 99%

Tropomyosin: A panallergen that causes a worldwide allergic problem

Papia

Bellia

Uasuf

2021

allergy asthma proc

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Background: Panallergens are proteins that take part in key processes of organisms and, therefore, are ubiquitously distributed with highly conserved sequences and structures. One class of these panallergens is composed of the tropomyosins. The highly heat-stable tropomyosins comprise the major allergens in crustaceans and mollusks, which make them important food allergens in exposed populations. Tropomyosins are responsible for a widespread immunoglobulin E cross-reactivity among allergens from different sources. Allergic tropomyosins are expressed in many species, including parasites and insects. Methods: This panallergen class is divided, according to it capacity of induced allergic symptoms, into allergenic or nonallergenic tropomyosin. Although vertebrate tropomyosins share ∼55% of sequence homology with invertebrate tropomyosins, it has been thought that the invertebrate tropomyosins would not have allergic properties. Nevertheless, in recent years, this opinion has been changed. In particular, tropomyosin has been recognized as a major allergen in many insects. Results: A high grade of homology has been shown among tropomyosins from different species, such as crustaceans and insects, which supports the hypothesis of cross-reactivity among tropomyosins from divergent species. Moreover, the emerging habit of consuming edible insects has drawn the attention of allergists to invertebrate tropomyosin protein due to its potential allergenic risk. Nevertheless, evidence about tropomyosin involvement in clinical allergic response is still scarce and deserves more investigation. Conclusion: This review intended to report allergic reactions associated with different tropomyosins when considering house dust mites, parasites, seafood, and insects, and to summarize our current knowledge about its cross-reactivity because this could help physicians to accurately diagnose patients with food allergy.

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“…Moreover, shellfish tropomyosin has multiple IgE‐binding sites that cross‐react with IgE from cockroaches and termites allergic patients. [ 6,7 ] Similarly, ovalbumin (OVA) comprises 54% of the protein in egg white, and is the main allergen in egg, frequently inducing allergic reactions especially in children. [ 8,9 ] The food allergy is a quite complicated physiological process involving various cell types such as the intestinal epithelial cell, dendritic cell, T cell, B cell, and mast cell, and is distinguished from other adverse reactions to food.…”

Section: Introductionmentioning

confidence: 99%

Suppression of Hippo Pathway by Food Allergen Exacerbates Intestinal Epithelia Instability and Facilitates Hypersensitivity

Wang

Lin

et al. 2020

Molecular Nutrition Food Res

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Scope Hippo signaling is a crucial pathway in innate immune responses, but the relationship between food allergy and Hippo pathway is unknown. The aim of this work is to investigate the regulation of food allergy by Hippo pathway and reveal the molecular mechanisms. Methods and results Two food allergens tropomyosin and ovalbumin are used to challenge a mouse model and CMT93 intestinal epithelia cell model. The allergic responses and the activation of Hippo pathway are tested in these models. In the mouse model, both allergens trigged significant allergic responses, and Hippo pathway is suppressed after allergen challenge. In CMT93, both allergens upregulate the expression of allergic cytokines thymic stromal lymphopoietin, interleukin (IL)‐25, and IL‐33. In TAZ KD CMT93, the Hippo pathway is blocked, and the expression of allergenic cytokines are also suppressed. Conclusions Both in vivo and in vitro data demonstrate that the two food allergens suppressed Hippo pathway by downregulating TAZ expression, resulting in intestinal epithelia instability, and finally leading to hypersensitivity reactions. These findings provide potential therapeutic targets and molecular markers for food allergy, and provide dietary guidelines for allergenic individuals.

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Cross-reaction of recombinant termite ( Coptotermes formosanus ) tropomyosin with IgE from cockroach and shrimp allergic individuals

Cited by 7 publications

References 10 publications

Genomics of Shrimp Allergens and Beyond

Genomics of Shrimp Allergens and Beyond

Tropomyosin: A panallergen that causes a worldwide allergic problem

Suppression of Hippo Pathway by Food Allergen Exacerbates Intestinal Epithelia Instability and Facilitates Hypersensitivity

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