Effects of the Maillard reaction on the epitopes and immunoreactivity of tropomyosin, a major allergen in<i>Chlamys nobilis</i>

Bai, Tian-Liang; Han, Xinyu; Li, Meng-Si; Yang, Yang; Liu, Meng; Ji, Nai-Ru; Yu, Chenchen; Lai, Dong; Cao, Min‐Jie

doi:10.1039/d1fo00270h

Cited by 29 publications

(47 citation statements)

References 39 publications

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“…Physicochemical properties, including thermal stability, pH stability, and in vitro digestibility, could influence the sensitization of allergens . Here, α-TM showed high thermal stability, which is consistent with scallop TM that remained stable even at 100 °C . However, α 2 -TM degraded to α-TM when the temperature was over 60 °C.…”

Section: Discussionsupporting

confidence: 67%

“…The Q-Sepharose was purchased from GE Healthcare (Waukesha, Wisconsin, USA). The rabbit Chlamys nobilis TM polyclonal antibody was prepared in our laboratory . Horseradish peroxidase-labeled goat anti-human IgE antibody and horseradish peroxidase-labeled anti-rabbit IgG antibody were obtained from Southern Biotech (Birmingham, Alabama, USA).…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

“…The western blot and dot blot were analyzed using Chlamys nobilis TM polyclonal antibody, as described by Bai et al (1:1 × 10 4 dilution), and abalone-sensitive patients’ sera (1:3 dilution) as the primary antibody. The Chlamys nobilis TM was prepared as positive control described by a previous study . Moreover, the target protein bands cut from the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) gel were sent to Shenzhen Wininnovate BIO (Shenzhen, Guangdong, China) and analyzed by LC–MS/MS.…”

Section: Methodsmentioning

confidence: 99%

“…The rabbit Chlamys nobilis TM polyclonal antibody was prepared in our laboratory. 26 Horseradish peroxidase-labeled goat anti-human IgE antibody and horseradish peroxidase-labeled anti-rabbit IgG antibody were obtained from Southern Biotech (Birmingham, Alabama, USA). Pepsin, trypsin, chymotrypsin, and 8-anilino-1-naphthalenesulfonic acid (ANS), and β-mercaptoethanol were purchased from Sigma-Aldrich (St Louis, Missouri, USA).…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

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Analysis of Immunoreactivity of α/α₂-Tropomyosin from Haliotis discus hannai, Based on IgE Epitopes and Structural Characteristics

Han

et al. 2021

J. Agric. Food Chem.

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Tropomyosin (TM) was reported to be a supercoil allergen of shellfish. However, little information is available about its link between structure and allergenicity. In this study, the subunit of TM (α-TM) and supercoil of TM (α 2 -TM) were identified from Haliotis discus hannai. α 2 -TM showed higher immunoreactivity than α-TM. Meanwhile, seven linear epitopes in α-TM and α 2 -TM were verified, and two conformational epitopes in α 2 -TM were predicted. The physicochemical properties and chemical bond assays confirmed the existence of the disulfide bond in α 2 -TM. According to spectroscopy and hydrophobicity analysis, α-TM showed higher α-helix features and blueshift of the fluorescence intensity peak compared with those of α 2 -TM. The structure analysis revealed the possibility of conformational epitopes in α 2 -TM, which could explain the immunoreactivity differences between α-TM and α 2 -TM further. These results improved the understanding of Haliotis discus hannai TM, which lay the foundation for the food processing of abalone.

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Section: Discussionsupporting

confidence: 67%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 99%

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Analysis of Immunoreactivity of α/α₂-Tropomyosin from Haliotis discus hannai, Based on IgE Epitopes and Structural Characteristics

Han

et al. 2021

J. Agric. Food Chem.

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Identification of major and cross‐reactive allergens of local freshwater snail (Pila polita) and the impact of thermal and non‐thermal food processing on allergen stability

et al. 2023

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BACKGROUND Snail allergy is rare but can be fatal. Pila polita, a freshwater snail, was considered as a popular exotic food, particularly in tropical countries, and consumed in processed forms. Thus, the purpose of this study was to identify the major and cross‐reactive allergens of P. polita and to determine the impact of food processing on the allergen stability. RESULTS Sodium dodecyl sulfate–polyacrylamide gel electrophoresis fractionated raw snail extract to approximately 24 protein bands, between 9 and 245 kDa. The prominent band at 33 kDa was detected in all raw and processed snail extracts. Immunoblotting tests of the raw extract demonstrated 19 immunoglobulin E (IgE)‐binding proteins, and four of them, at 30, 35, 42 and 49 kDa, were revealed as the major IgE‐binding proteins of P. polita. Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry identified the 49 and 42 kDa major allergens as actin, whereas the 30 and 35 kDa major allergens were identified as tropomyosin. Immunoblotting revealed that the raw snail had more allergenic proteins than the processed snail. The degree of allergenicity in decreasing order was raw > brine pickled> boiled > roasted > fried > vinegar pickled. The presence of cross‐reactivity between P. polita and the shellfish tested was exhibited with either no, complete, or partial inhibitions. CONCLUSION Actin and tropomyosin were identified as the major and cross‐reactive allergens of P. polita among local patients with snail allergy. Those major allergens are highly stable to high temperatures, acidic pH, and high salt, which might played a crucial role in snail allergy in Malaysia. © 2023 Society of Chemical Industry.

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Allergen Stability in Food Allergy: A Clinician’s Perspective

Koidl,

Gentile,

Untersmayr

2023

Curr Allergy Asthma Rep

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Purpose of Review The globally rising food allergy prevalence is associated with the urgent need for new disease prevention methods, efficient treatment, and reliable risk assessment methods for characterization of food allergens. Due to inter-individual variations in the digestive system, food allergens are degraded to a different extent in each person. Food processing also influences allergen digestion. Recent Findings In this review, we provide an overview of the digestive system with focus on relevance for food allergy. Main food proteins causing allergic reactions are evaluated, and the combined role of food processing and digestion for allergen stability is highlighted. Finally, clinical implications of this knowledge are discussed. Summary Recent literature shows that allergen digestibility is dependent on food processing, digestive conditions, and food matrix. Digestion affects proteins allergenicity. It is currently not possible to predict the immunogenicity of allergens solely based on protein stability.

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Effects of the Maillard reaction on the epitopes and immunoreactivity of tropomyosin, a major allergen inChlamys nobilis

Abstract: Scallop (Chlamys nobilis) cause IgE mediated food allergy, however, studies on allergens in its musculus are not comprehensive enough. In this connection, the target protein was purified from scallop and...

Cited by 29 publications

References 39 publications

Analysis of Immunoreactivity of α/α₂-Tropomyosin from Haliotis discus hannai, Based on IgE Epitopes and Structural Characteristics

Analysis of Immunoreactivity of α/α₂-Tropomyosin from Haliotis discus hannai, Based on IgE Epitopes and Structural Characteristics

Identification of major and cross‐reactive allergens of local freshwater snail (Pila polita) and the impact of thermal and non‐thermal food processing on allergen stability

Allergen Stability in Food Allergy: A Clinician’s Perspective

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Effects of the Maillard reaction on the epitopes and immunoreactivity of tropomyosin, a major allergen inChlamys nobilis

Abstract: Scallop (Chlamys nobilis) cause IgE mediated food allergy, however, studies on allergens in its musculus are not comprehensive enough. In this connection, the target protein was purified from scallop and...

Cited by 29 publications

References 39 publications

Analysis of Immunoreactivity of α/α2-Tropomyosin from Haliotis discus hannai, Based on IgE Epitopes and Structural Characteristics

Analysis of Immunoreactivity of α/α2-Tropomyosin from Haliotis discus hannai, Based on IgE Epitopes and Structural Characteristics

Identification of major and cross‐reactive allergens of local freshwater snail (Pila polita) and the impact of thermal and non‐thermal food processing on allergen stability

Allergen Stability in Food Allergy: A Clinician’s Perspective

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Analysis of Immunoreactivity of α/α₂-Tropomyosin from Haliotis discus hannai, Based on IgE Epitopes and Structural Characteristics

Analysis of Immunoreactivity of α/α₂-Tropomyosin from Haliotis discus hannai, Based on IgE Epitopes and Structural Characteristics