Shrimp tropomyosin retains antibody reactivity after exposure to acidic condition

Lasekan, Adeseye; Cao, Hanjuan; Maleki, Soheila J.; Nayak, Balunkeswar

doi:10.1002/jsfa.8221

Cited by 7 publications

(3 citation statements)

References 35 publications

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“…Under extreme heat load, the denaturation of TM occurs, the heat‐denatured TM can then be refolded upon cooling and the antigenicity remains after the heat processing (Z. Zhang et al., 2021). The antigenicity also remains after acid treatment (Lasekan et al., 2017).…”

Section: Tm: Molecular Characterization Epitopes and Cross‐reactivitymentioning

confidence: 99%

An overview of tropomyosin as an important seafood allergen: Structure, cross‐reactivity, epitopes, allergenicity, and processing modifications

Cheng

Wang

Sun

2021

Comp Rev Food Sci Food Safe

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Tropomyosin (TM) is a major allergen in crustaceans, which often causes allergy and is fatal to some consumers. Currently, the most effective treatment is to avoid ingesting TM, although most adverse events occur in accidental ingestion. In this review, the molecular characterization, epitopes, cross‐reactivity, and pathogenesis of TM are introduced and elucidated. Modification of TM by traditional processing methods such as heat treatment and enzymatic hydrolysis, and innovative processing technologies including high‐pressure treatment, cold plasma (CP), ultrasound, pulsed electric field (PEF), pulsed ultraviolet, microwave and irradiation are discussed in detail. Particularly, enzymolysis, PEF, and CP technologies show great potential for modifying TM and more studies are needed to verify their effectiveness for the seafood industry. Possible mechanisms and the advantages/disadvantages of these technologies for the mitigation of TM allergenicity are also highlighted. Further work should be conducted to investigate the allergenicity caused by protein segments such as epitopes, examine the interaction sites between the allergen and the processing techniques and reveal the reduction mechanism of allergenicity.

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Section: Tm: Molecular Characterization Epitopes and Cross‐reactivitymentioning

confidence: 99%

An overview of tropomyosin as an important seafood allergen: Structure, cross‐reactivity, epitopes, allergenicity, and processing modifications

Cheng

Wang

Sun

2021

Comp Rev Food Sci Food Safe

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“…They stated that the loss of pancreatic enzymes occurred when the gastric acid level determined the activation of the gastric pepsin. Thus, when the antacid drug prevents the gastric acid, there is a possibility that the allergic reaction will be increased drastically [77].…”

Section: Acid Processingmentioning

confidence: 99%

Effects of Food Processing on the Stability and Quality of Shellfish Allergens

Ali¹,

Rosmilah²

2019

UCMS

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The high number of allergens that exist in the human food supply had led to increment of food allergies awareness by taking suitable prevention to protect sensitive consumers from unsolicited exposures to food allergens. Several attempts were done to lessen or eradicate the food allergenicity via food processing which eventually resulted in mixed outcomes. The rationale behind the usage of food processing to reduce/remove the food allergenicity and the limitations encountered are further discussed.

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“…The homology of TM amino acid sequences ranges from 93% to 99% in crustaceans 4 with a molecular weight of approximately 35 kDa. To date, TM has been identified in numerous invertebrate species, such as crustaceans (lobster, 5 prawn, 6 shrimp, 7 crab 8 ), mollusks, 9 cockroaches 10 and mites 11 . TM from M. nipponense ( Mn TM) was previously purified and identified in our laboratory.…”

Section: Introductionmentioning

confidence: 99%

Characterization of systemic allergenicity of tropomyosin from shrimp (Macrobrachium nipponense) and anaphylactic reactions in digestive tract

Xie

Shao

et al. 2020

J Sci Food Agric

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BACKGROUND Tropomyosin (TM) is the major allergen of crustaceans. The allergenicity of TM from Macrobrachium nipponense (MnTM) and the anaphylactic reaction in the digestive tract are still unclear. The aim of this study was to evaluate the allergenicity of MnTM and the anaphylactic reaction in the digestive tract. RESULTS Serum IgE and IgG1 binding ability in the TM group were significantly higher than those in the PBS and CT groups (P < 0.01) and CP group (P < 0.05), while serum IgG and IgG2a binding ability showed no obvious difference between the four groups (P > 0.05). The levels of cytokines IL‐4, IL‐5 and IL‐13 in TM and CP groups were significantly higher than those in PBS and CT groups. Histamine and β‐hexosaminidase in the TM and CP groups from basophil cell models were significantly higher than those in the PBS group. The highest mRNA expression of IL‐4 and IL‐13 was in the jejunum from TM‐sensitized mice. Histopathological analysis showed that more immune cells infiltrated into the jejunum than the duodenum and ileum from the TM‐sensitized mice. CONCLUSIONS MnTM could promote an allergic response in mice and lead to degranulation in basophil cells. The jejunum was more easily affected by MnTM than duodenum and ileum, and the jejunum may be the major site of allergic response in the digestive tract. © 2020 Society of Chemical Industry

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Shrimp tropomyosin retains antibody reactivity after exposure to acidic condition

Cited by 7 publications

References 35 publications

An overview of tropomyosin as an important seafood allergen: Structure, cross‐reactivity, epitopes, allergenicity, and processing modifications

An overview of tropomyosin as an important seafood allergen: Structure, cross‐reactivity, epitopes, allergenicity, and processing modifications

Effects of Food Processing on the Stability and Quality of Shellfish Allergens

Characterization of systemic allergenicity of tropomyosin from shrimp (Macrobrachium nipponense) and anaphylactic reactions in digestive tract

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