Identification of physicochemical properties of <i>Scylla paramamosain</i> allergen, arginin kinase

Yu, Huilin; Ruan, Wei-Wei; Cao, Min‐Jie; Cai, Qiu-Feng; Shen, Hai-Wang

doi:10.1002/jsfa.5748

Cited by 20 publications

(15 citation statements)

References 39 publications

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“…This investigation showed that the high molecular weight band corresponding to haemocyanin in the raw extract was not observed in the cooked extract. Arginine kinase was also not identified within the cooked mud crab extract, consistent with being heat labile as documented previously for other crab species [30, 31]. However, there was also evidence for heat stable proteins such as tropomyosin, with mud crab tropomyosin retaining IgE reactivity as a monomer, aggregate and fragment in the cooked extract.…”

Section: Discussionsupporting

confidence: 82%

Effect of thermal processing on T cell reactivity of shellfish allergens - Discordance with IgE reactivity

et al. 2017

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Crustacean allergy is a major cause of food-induced anaphylaxis. We showed previously that heating increases IgE reactivity of crustacean allergens. Here we investigate the effects of thermal processing of crustacean extracts on cellular immune reactivity. Raw and cooked black tiger prawn, banana prawn, mud crab and blue swimmer crab extracts were prepared and IgE reactivity assessed by ELISA. Mass spectrometry revealed a mix of several allergens in the raw mud crab extract but predominant heat-stable tropomyosin in the cooked extract. PBMC from crustacean-allergic and non-atopic control subjects were cultured with the crab and prawn extracts and proliferation of lymphocyte subsets was analysed by CFSE labelling and flow cytometry. Effector responses were assessed by intracellular IL-4 and IFN-γ, and regulatory T (CD4+CD25+CD127loFoxp3+) cell proportions in cultures were also compared by flow cytometry. For each crustacean species, the cooked extract had greater IgE reactivity than the raw (mud crab p<0.05, other species p<0.01). In contrast, there was a trend for lower PBMC proliferative responses to cooked compared with raw extracts. In crustacean-stimulated PBMC cultures, dividing CD4+ and CD56+ lymphocytes showed higher IL-4+/IFN-γ+ ratios for crustacean-allergic subjects than for non-atopics (p<0.01), but there was no significant difference between raw and cooked extracts. The percentage IL-4+ of dividing CD4+ cells correlated with total and allergen-specific IgE levels (prawns p<0.01, crabs p<0.05). Regulatory T cell proportions were lower in cultures stimulated with cooked compared with raw extracts (mud crab p<0.001, banana prawn p<0.05). In conclusion, cooking did not substantially alter overall T cell proliferative or cytokine reactivity of crustacean extracts, but decreased induction of Tregs. In contrast, IgE reactivity of cooked extracts was increased markedly. These novel findings have important implications for improved diagnostics, managing crustacean allergy and development of future therapeutics. Assessment of individual allergen T cell reactivity is required.

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Section: Discussionsupporting

confidence: 82%

Effect of thermal processing on T cell reactivity of shellfish allergens - Discordance with IgE reactivity

et al. 2017

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“…In contrast, arginine kinase is a globular protein, which tends to unfold during heating, exposing hydrophobic amino acids, which are normally inside the protein. The exposed hydrophobic amino acids from different molecules will interact in such a way, that formation of larger protein aggregates will occur [25]. Cross-linking of arginine kinase may also be caused by polyphenol oxidase-mediated cross-linking.…”

Section: Discussionmentioning

confidence: 99%

Effect of thermal processing on mealworm allergenicity

Broekman

Knulst

Jäger

et al. 2015

Molecular Nutrition Food Res

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“…Similar to tropomyosin, arginine kinase is highly abundant in invertebrate muscle, and hitherto, it has also been described in various other shellfish species as well as other invertebrates such as mites, cockroaches, crickets, silk worms, and the Indian meal moth . Unlike tropomyosins, they display unstable physicochemical properties and do not resist thermal and acid‐base treatment .…”

Section: Allergensmentioning

confidence: 99%

Shellfish allergens: tropomyosin and beyond

Faber

Pascal

Kharbouchi

et al. 2017

Allergy

132

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IgE-mediated shellfish allergy constitutes an important cause of food-related adverse reactions. Shellfish are classified into mollusks and crustaceans, the latter belonging to the class of arthropoda. Among crustaceans, shrimps are the most predominant cause of allergic reactions and thus more extensively studied. Several major and minor allergens have been identified and cloned. Among them, invertebrate tropomyosin, arginine kinase, myosin light chain, sarcoplasmic calciumbinding protein, and hemocyanin are the most relevant. This review summarizes our current knowledge about these allergens.IgE-mediated shellfish allergy constitutes an important and increasing health issue in both children and adults (1, 2). During the last two decades, significant progress in biochemistry and molecular biology enabled the characterization, cloning, and recombinant production of various shellfish allergen components and epitope-emulating peptides that might become available for quantification of specific IgE (sIgE) antibodies, namely molecular diagnosis. This review intends to summarize our current knowledge about shellfish allergens and their cross-reactivity as this might be the key to optimize diagnosis (3, 4). Table 1 summarizes the most relevant shellfish allergens that have currently been characterized. Tropomyosin is considered to be the major allergen in shellfish allergy. Actually, already in the early 1980s Hoffman et al. (5) identified a heat-stable IgE-binding allergen in shrimps that was later identified as tropomyosin in brown shrimp (Penaeus aztecus) reacting with 28/ 34 (82%) of shrimp-sensitive individuals (6). Moreover, tropomyosin has been identified as a panallergen of many invertebrate species including other crustaceans (lobster, crab), mollusks (mussels, oysters, scallops, octopus, squids, snails, abalones, whelk, clams, razor shell), cockroaches, and mites (7-18). Tropomyosins are present in both muscle and nonmuscle cells. In striated muscle, they mediate the interaction of troponin-actin complex to regulate contraction. Note that tropomyosins from crustaceans share a high homology (up to 98%), whereas the amino acid sequence identity between (3,(19)(20)(21)(22)(23)(24)(25). Children were once reported to recognize a greater epitope repertoire than adults and thus suggested that shrimp sensitization could decrease over age (22). However, more recent studies with challenged patients could not reproduce this observation with the same epitope mapping (3, 24). About one decade ago, a recombinant tropomyosin from Penaeus aztecus, rPen a 1, became commercially available for molecular diagnostic testing, with improved results as a diagnostic tool in comparison with the whole-shrimp extract (26,27). In addition to tropomyosin, several other allergenic components have been identified in shellfish. In 2003, Yu et al. identified a novel allergen in Penaeus monodon (black tiger shrimp) (28), designated as Pen m 2, with arginine kinase activity. Similar to tropomyosin, arginine kinase is highly abundant i...

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Identification of physicochemical properties of Scylla paramamosain allergen, arginin kinase

Abstract: AK is an important food allergen despite its unstable physicochemical properties of digestibility.

Cited by 20 publications

References 39 publications

Effect of thermal processing on T cell reactivity of shellfish allergens - Discordance with IgE reactivity

Effect of thermal processing on T cell reactivity of shellfish allergens - Discordance with IgE reactivity

Effect of thermal processing on mealworm allergenicity

Shellfish allergens: tropomyosin and beyond

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