Alpha-amylase as the culprit in an occupational mealworm allergy case.
alpha-amylase
edible insect
mealworm
occupational asthma
tenebrio molitor
Journal
Frontiers in allergy
ISSN: 2673-6101
Titre abrégé: Front Allergy
Pays: Switzerland
ID NLM: 9918227355906676
Informations de publication
Date de publication:
2022
2022
Historique:
received:
12
07
2022
accepted:
11
08
2022
entrez:
16
9
2022
pubmed:
17
9
2022
medline:
17
9
2022
Statut:
epublish
Résumé
Occupational allergy has been described in employees working in contact with mealworms in pet stores, live fish bait or infested stored grains and recently, in mealworm farming for animal feed and human consumption. Mealworm allergens linked to occupational allergy are troponin C, cockroach-like allergen, tropomyosin, arginine kinase, early-staged encapsulation inducing- and larval cuticle proteins. We report a case of occupational mealworm allergy and studied the culprit component. Diagnosis was done by skin prick, specific IgE, basophil activation and lung function testing. Allergen purification was performed by anion-exchange chromatography and immunoblotting with patient IgE. Allergens were identified by in-gel trypsin digest and tandem mass spectrometry. Allergenicity and specificity further confirmed by IgE inhibition and passive basophil activation experiments. We describe a new case of occupational mealworm allergy in a laboratory worker, with sensitization to different developmental stages and derivates of the mealworm. In basophil activation tests, the majority of patient's basophils (69%-91%) degranulated upon stimulation with the lowest concentration of mealworm extracts (0.16 µg/ml). Despite strong sensitization to mites, the patient did not show cross-reactivity to other insects. We were able to identify alpha-amylase as the main allergen and through inhibition experiments, we demonstrated that low amounts (0.1 µg/ml) of this allergen could strongly inhibit mealworm specific IgE by 79.1%. Moreover, passive BAT experiments demonstrated the IgE-alpha-amylase interaction to be functional, inducing up to 25.5% degranulation in healthy donor basophils. Alpha-amylase can be identified as the responsible allergen in this specific case of occupational mealworm allergy.
Sections du résumé
Background
UNASSIGNED
Occupational allergy has been described in employees working in contact with mealworms in pet stores, live fish bait or infested stored grains and recently, in mealworm farming for animal feed and human consumption. Mealworm allergens linked to occupational allergy are troponin C, cockroach-like allergen, tropomyosin, arginine kinase, early-staged encapsulation inducing- and larval cuticle proteins.
Objective
UNASSIGNED
We report a case of occupational mealworm allergy and studied the culprit component.
Methods
UNASSIGNED
Diagnosis was done by skin prick, specific IgE, basophil activation and lung function testing. Allergen purification was performed by anion-exchange chromatography and immunoblotting with patient IgE. Allergens were identified by in-gel trypsin digest and tandem mass spectrometry. Allergenicity and specificity further confirmed by IgE inhibition and passive basophil activation experiments.
Results
UNASSIGNED
We describe a new case of occupational mealworm allergy in a laboratory worker, with sensitization to different developmental stages and derivates of the mealworm. In basophil activation tests, the majority of patient's basophils (69%-91%) degranulated upon stimulation with the lowest concentration of mealworm extracts (0.16 µg/ml). Despite strong sensitization to mites, the patient did not show cross-reactivity to other insects. We were able to identify alpha-amylase as the main allergen and through inhibition experiments, we demonstrated that low amounts (0.1 µg/ml) of this allergen could strongly inhibit mealworm specific IgE by 79.1%. Moreover, passive BAT experiments demonstrated the IgE-alpha-amylase interaction to be functional, inducing up to 25.5% degranulation in healthy donor basophils.
Conclusion
UNASSIGNED
Alpha-amylase can be identified as the responsible allergen in this specific case of occupational mealworm allergy.
Identifiants
pubmed: 36110144
doi: 10.3389/falgy.2022.992195
pmc: PMC9468247
doi:
Types de publication
Journal Article
Langues
eng
Pagination
992195Informations de copyright
© 2022 Ganseman, Ieven, Frans, Coorevits, Pörtner, Martens, Bullens, Schrijvers, Breynaert and Proost.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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