Limited cross reactivity among arginine kinase allergens from mealworm and cricket edible insects

Francis, Frédéric; Doyen, Virginie; Debaugnies, F.; Mazzucchelli, Gabriel; Caparros, Rudy; Alabi, Taofic; Blecker, Christophe; Haubruge, Éric; Corazza, Francis

doi:10.1016/j.foodchem.2018.10.082

Cited by 49 publications

(32 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…More recently, an anaphylactic reaction was reported after consumption of yellow mealworm [34], and silkworm pupae [35]. Most of the insect allergens identified as IgE-binding allergens, cross-react with shellfish, mollusk and nematod allergens and thus correspond to IgEbinding cross-reacting pan-allergens, widely distributed in various animal phyla [36][37][38][39][40][41][42][43][44]. Among these cross-reacting allergens, alpha-actin, arginine-kinase (AK), enolase, fructose-1,6-biphosphate aldolase (FPA), glyceraldehyde-3-phopho-deshydrogenase (GAPDH), and tropomyosin, consist of the frequently identified IgE-binding cross-reacting allergens [33].…”

Section: Introductionmentioning

confidence: 99%

A Proteomic- and Bioinformatic-Based Identification of Specific Allergens from Edible Insects: Probes for Future Detection as Food Ingredients

Barre

Pichereaux

Simplicien

et al. 2021

Foods

View full text Add to dashboard Cite

The increasing development of edible insect flours as alternative sources of proteins added to food and feed products for improving their nutritional value, necessitates an accurate evaluation of their possible adverse side-effects, especially for individuals suffering from food allergies. Using a proteomic- and bioinformatic-based approach, the diversity of proteins occurring in currently consumed edible insects such as silkworm (Bombyx mori), cricket (Acheta domesticus), African migratory locust (Locusta migratoria), yellow mealworm (Tenebrio molitor), red palm weevil (Rhynchophorus ferrugineus), and giant milworm beetle (Zophobas atratus), was investigated. Most of them consist of phylogenetically-related protein allergens widely distributed in the different groups of arthropods (mites, insects, crustaceans) and mollusks. However, a few proteins belonging to discrete protein families including the chemosensory protein, hexamerin, and the odorant-binding protein, emerged as proteins highly specific for edible insects. To a lesser extent, other proteins such as apolipophorin III, the larval cuticle protein, and the receptor for activated protein kinase, also exhibited a rather good specificity for edible insects. These proteins, that are apparently missing or much less represented in other groups of arthropods, mollusks and nematods, share well conserved amino acid sequences and very similar three-dimensional structures. Owing to their ability to trigger allergic responses in sensitized people, they should be used as probes for the specific detection of insect proteins as food ingredients in various food products and thus, to assess their food safety, especially for people allergic to edible insects.

show abstract

Section: Introductionmentioning

confidence: 99%

A Proteomic- and Bioinformatic-Based Identification of Specific Allergens from Edible Insects: Probes for Future Detection as Food Ingredients

Barre

Pichereaux

Simplicien

et al. 2021

Foods

View full text Add to dashboard Cite

show abstract

“…Small differences in the sequences could likely cause a differential IgE binding, as Palmer and collaborators also stated [ 51 ••]. This could be the reason for the absence of cross-reactivity observed by Francis and co-workers [ 50 ••].…”

Section: Cross-reactivity and Primary Sensitizationmentioning

confidence: 97%

“…However, cross-reactivity seems not to be systematic. Francis et al [ 50 ••] investigated the cross-reactivity of AK from A. domesticus and T. molitor in subjects exposed to edible insects, and no cross-reaction phenomena were observed, although AK from different insects are acknowledged to share high sequence identity (70% on average) and homology (90% on average) [ 37 ]. Small differences in the sequences could likely cause a differential IgE binding, as Palmer and collaborators also stated [ 51 ••].…”

Section: Cross-reactivity and Primary Sensitizationmentioning

confidence: 99%

Allergens from Edible Insects: Cross-reactivity and Effects of Processing

Marchi

Wangorsch

Zoccatelli

2021

Curr Allergy Asthma Rep

View full text Add to dashboard Cite

Purpose of Review The recent introduction of edible insects in Western countries has raised concerns about their safety in terms of allergenic reactions. The characterization of insect allergens, the sensitization and cross-reactivity mechanisms, and the effects of food processing represent crucial information for risk assessment. Recent Findings Allergic reactions to different insects and cross-reactivity with crustacean and inhalant allergens have been described, with the identification of new IgE-binding proteins besides well-known pan-allergens. Depending on the route of sensitization, different potential allergens seem to be involved. Food processing may affect the solubility and the immunoreactivity of insect allergens, with results depending on species and type of proteins. Chemical/enzymatic hydrolysis, in some cases, abolishes immunoreactivity. Summary More studies based on subjects with a confirmed insect allergy are necessary to identify major and minor allergens and the role of the route of sensitization. The effects of processing need to be further investigated to assess the risk associated with the ingestion of insect-containing food products.

show abstract

“…Enzymatic hydrolysis was used as an appropriate treatment to reduce the allergenic risk in lesser mealworms [ 68 ]. On the other hand, arginine kinase from mealworms and crickets commercially available was assessed, showing a low specific reactivity of this allergen [ 69 ].…”

Section: Food Allergens In Vegetable and Animal Productsmentioning

confidence: 99%

Current Trends in Proteomic Advances for Food Allergen Analysis

López‐Pedrouso

Lorenzo

Gagaoua

2020

Biology

View full text Add to dashboard Cite

Food allergies are a global food challenge. For correct food labelling, the detection and quantification of allergens are necessary. However, novel product formulations and industrial processes produce new scenarios, which require much more technological developments. For this purpose, OMICS technologies, especially proteomics, seemed to be relevant in this context. This review summarises the current knowledge and studies that used proteomics to study food allergens. In the case of the allergenic proteins, a wide variety of isoforms, post-translational modifications and other structural changes during food processing can increase or decrease the allergenicity. Most of the plant-based food allergens are proteins with biological functions involved in storage, structure, and plant defence. The allergenicity of these proteins could be increased by the presence of heavy metals, air pollution, and pesticides. Targeted proteomics like selected/multiple reaction monitoring (SRM/MRM) have been very useful, especially in the case of gluten from wheat, rye and barley, and allergens from lentil, soy, and fruit. Conventional 1D and 2-DE immunoblotting have been further widely used. For animal-based food allergens, the widely used technologies are 1D and 2-DE immunoblotting followed by MALDI-TOF/TOF, and more recently LC-MS/MS, which is becoming useful to assess egg, fish, or milk allergens. The detection and quantification of allergenic proteins using mass spectrometry-based proteomics are promising and would contribute to greater accuracy, therefore improving consumer information.

show abstract

Limited cross reactivity among arginine kinase allergens from mealworm and cricket edible insects

Cited by 49 publications

References 23 publications

A Proteomic- and Bioinformatic-Based Identification of Specific Allergens from Edible Insects: Probes for Future Detection as Food Ingredients

A Proteomic- and Bioinformatic-Based Identification of Specific Allergens from Edible Insects: Probes for Future Detection as Food Ingredients

Allergens from Edible Insects: Cross-reactivity and Effects of Processing

Current Trends in Proteomic Advances for Food Allergen Analysis

Contact Info

Product

Resources

About