Assessment of the sensitizing capacity and allergenicity of enzymatic cross‐linked arginine kinase, the crab allergen

Fei, Dan-Xia; Liu, Qingmei; Chen, Feng; Yang, Yang; Chen, Zhongwei; Cao, Min‐Jie; Liu, Guangming

doi:10.1002/mnfr.201500936

Cited by 48 publications

(61 citation statements)

References 38 publications

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“…The reduction in the allergenicity of turbot PV via Tyr and CA are consistent with the changes in the structural properties. Structural changes might cause the modification of amino acid residues and binding epitopes, which agreed with the results reported in recent studies . Fei et al did some research on crosslinked thermal polymerized arginine kinase (AK) and analyzed the potential allergenicity.…”

Section: Resultssupporting

confidence: 81%

“…Structural changes might cause the modification of amino acid residues and binding epitopes, which agreed with the results reported in recent studies. 13,25,45 Fei et al 45 did some research on crosslinked thermal polymerized arginine kinase (AK) and analyzed the potential allergenicity. According to the results of inhibition ELISA, the half inhibitory concentration of AK after crosslinking changed from 1.13 to 228.36 μg mL −1 and the binding activity of crosslinked thermal polymerized AK reduced.…”

Section: Igg Binding Analysis Of Crosslinked Pvmentioning

confidence: 99%

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Effect of tyrosinase‐catalyzed crosslinking on the structure and allergenicity of turbot parvalbumin mediated by caffeic acid

Tian

Ahmed

et al. 2019

J Sci Food Agric

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BACKGROUND Enzymatic treatment of allergenic protein can alter their functional properties under a mild reaction condition due to specificity of enzymes. Phenolic compounds act as mediators and enhance the crosslinking reactions. The study aimed to assess the changes in the structure and immunoglobulin G (IgG) binding capacity of turbot parvalbumin (PV) upon crosslinking with tyrosinase (Tyr) in the absence and presence of caffeic acid. RESULTS Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) analysis revealed the appearance of higher molecular weight bands (24, 36 kDa) in the crosslinked PV. The secondary structure of crosslinked PV became loosened and disordered. The results of intrinsic fluorescence and ultraviolet absorption spectral analyses, as well as surface hydrophobicity and free amino group analyses also revealed structural changes. As observed by western blot analysis, the intensity of the PV bands reduced upon Tyr treatment, indicating reduced binding of specific IgG to PV. Moreover, the indirect ELISA (enzyme‐linked immunosorbent assay) analysis confirmed that the IgG binding ability of crosslinked PV was reduced 34.94%. CONCLUSION Enzymatic treatment mitigated the allergenicity of fish PV, which was closely related to the alterations in the conformational structure. This treatment showed potential for developing hypoallergenic fish products under mild reaction conditions. © 2019 Society of Chemical Industry

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Section: Resultssupporting

confidence: 81%

Section: Igg Binding Analysis Of Crosslinked Pvmentioning

confidence: 99%

Effect of tyrosinase‐catalyzed crosslinking on the structure and allergenicity of turbot parvalbumin mediated by caffeic acid

Tian

Ahmed

et al. 2019

J Sci Food Agric

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“…Thus, CTC and CHP preferentially induced Th1-and/or Treg-oriented immune response in vivo. Additionally, the group employed the same strategy and demonstrated that cross-linking arginine kinase from crab with horseradish peroxidase or tyrosinase also significantly reduced its allergenicity and promoted its capacity in inducing oral tolerance in mice [70]. Clinical trials regarding the safety and efficacies of these enzyme cross-linked allergens in treating crab allergy are imminent.…”

Section: Chemical Modificationmentioning

confidence: 99%

Overcoming Shellfish Allergy: How Far Have We Come?

Wai

Leung

Chu

et al. 2020

IJMS

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Shellfish allergy caused by undesirable immunological responses upon ingestion of crustaceans and mollusks is a common cause of food allergy, especially in the Asia-Pacific region. While the prevalence of shellfish allergy is increasing, the mainstay of clinical diagnosis for these patients includes extract-based skin prick test and specific IgE measurement while clinical management consists of food avoidance and as-needed use of adrenaline autoinjector should they develop severe allergic reactions. Such a standard of care is unsatisfactory to both patients and healthcare practitioners. There is a pressing need to introduce more specific diagnostic methods, as well as effective and safe therapies for patients with shellfish allergy. Knowledge gained on the identifications and defining the immuno-molecular features of different shellfish allergens over the past two decades have gradually translated into the design of new diagnostic and treatment options for shellfish allergy. In this review, we will discuss the epidemiology, the molecular identification of shellfish allergens, recent progress in various diagnostic methods, as well as current development in immunotherapeutic approaches including the use of unmodified allergens, hypoallergens, immunoregulatory peptides and DNA vaccines for the prevention and treatment of shellfish allergy. The prospect of a “cure “for shellfish allergy is within reach.

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“…A large number of literatures have proved that enzymatic cross-linking can reduce the binding activity of IgE to allergens. For example, cross-linking with laccase can effectively reduce the allergenicity of casein in milk (Tantoush et al, 2011); similarly, cross-linking with tyrosinase and caffeic acid decreased the binding activity of peanut allergen (Chung, Kato, & Champagne, 2010;Fei et al, 2016); furthermore, transglutaminase treatment can significantly reduce the allergenicity of milk and wheat allergens (Łącka & Bryszewska, 2006;F. Z. Yuan et al, 2018).…”

Section: Discussionmentioning

confidence: 99%

Transglutaminase-catalysed cross-linking eliminates Penaeus chinensis tropomyosin allergenicity by altering protein structure

Wang

et al. 2019

Food and Agricultural Immunology

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Transglutaminase (TG) is a major food processing enzyme that induces protein cross-linking. Tropomyosin (TM) is a major shellfish allergen that is responsible for at least 80% of the shrimp allergic incidents. The aim of this research was to investigate the effect of TG on TM allergenicity and reveal the involvement of TM structure alternation. After treated with TG for different time, the allergenicity of TM was assessed by indirect ELISA with shrimp allergic patients' sera, and the structure of TM was characterized by circular dichroism (CD) spectroscopy, ultraviolet (UV) absorption spectroscopy and fluorescence spectroscopy. Results showed that the allergenicity slightly decreased at the early stage of reaction and dramatically decreased at the late stage, which is tightly correlated with the increment of β-turn content and UV absorption. In conclusion, TG modification is an effective and promising food processing method to eliminate TM allergenicity with significant prospect of industrial application. ARTICLE HISTORY

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Assessment of the sensitizing capacity and allergenicity of enzymatic cross‐linked arginine kinase, the crab allergen

Abstract: Enzymatic cross-linking with thermal polymerization of AK by tyrosinase and caffeic acid had high potential in mitigating IgE-binding activity and allergenicity, which were influenced by altering the molecular and immunological features of the shellfish protein.

Cited by 48 publications

References 38 publications

Effect of tyrosinase‐catalyzed crosslinking on the structure and allergenicity of turbot parvalbumin mediated by caffeic acid

Effect of tyrosinase‐catalyzed crosslinking on the structure and allergenicity of turbot parvalbumin mediated by caffeic acid

Overcoming Shellfish Allergy: How Far Have We Come?

Transglutaminase-catalysed cross-linking eliminates Penaeus chinensis tropomyosin allergenicity by altering protein structure

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