In silico prediction and IgE serum screening for potential allergenicity of novel foods—a case of fungal biomass Fermotein®
Abstract
The fungus Rhizomucor pusillus CBS 143028 is the source of a novel food called Fermotein®, a whole fungal biomass rich in proteins, fibres, and micronutrients. To enable Fermotein® to enter the food market, the safety of the microorganism needs to be carefully assessed, including studying the allergenicity potential of proteins encoded by its genome. An in silico allergen database screening identified 23 proteins with more than 50% sequence identity over their full sequence, with proteins from food origin requiring allergen labelling in the European Union. These proteins are present in fish, crustaceans (e.g., shrimp, crab), peanuts, pistachio nuts, sesame seeds, and wheat. To unequivocally establish the likelihood of potential cross-reactivity of the proteins present in the novel food with those established allergens, sera of patients with doctor-diagnosed allergies to these six food categories were screened using ImmunoCAP technology. Of the 106 sera samples tested, 16 showed low IgE binding to Fermotein®. In 11 out of the 16 sera, it was demonstrated by IgE inhibition assays with Proteinase K-digested Fermotein® that all reactivity was directed to fungal carbohydrate moieties. For the remaining five sera, ImmunoCAP inhibition assays with the relevant allergen extracts and with purified human proteins highly homologous to the implicated allergen molecules demonstrated that there was no evidence to support significant cross-reactivity with the potential allergens identified in the bioinformatics in silico search. It is clear that IgE recognition of Fermotein® is dominated by clinically irrelevant carbohydrates. Based on these analyses, it is safe to conclude that Fermotein® presents a negligible allergenicity risk for food-allergic patients because the observed bioinformatics hits did not translate into IgE cross-reactivity.
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BibTeX
@article{versteeg2026silico,
title = {{In silico prediction and IgE serum screening for potential allergenicity of novel foods—a case of fungal biomass Fermotein®}},
author = {Serge Versteeg and Jaap Akkerdaas and Lucie Pařenicová and Martine Morisset and Wieneke Dijk and Andrea O'Malley and Yvonne Dommels and Ronald van Ree},
journal = {Frontiers in Allergy},
year = {2026},
month = may,
doi = {10.3389/falgy.2026.1746353},
url = {https://hal.science/hal-05779946v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - In silico prediction and IgE serum screening for potential allergenicity of novel foods—a case of fungal biomass Fermotein®
AU - Serge Versteeg
AU - Jaap Akkerdaas
AU - Lucie Pařenicová
AU - Martine Morisset
AU - Wieneke Dijk
AU - Andrea O'Malley
AU - Yvonne Dommels
AU - Ronald van Ree
PY - 2026
DA - 2026/05/18
JO - Frontiers in Allergy
DO - 10.3389/falgy.2026.1746353
UR - https://hal.science/hal-05779946v1
AB - The fungus Rhizomucor pusillus CBS 143028 is the source of a novel food called Fermotein®, a whole fungal biomass rich in proteins, fibres, and micronutrients. To enable Fermotein® to enter the food market, the safety of the microorganism needs to be carefully assessed, including studying the allergenicity potential of proteins encoded by its genome. An in silico allergen database screening identified 23 proteins with more than 50% sequence identity over their full sequence, with proteins from food origin requiring allergen labelling in the European Union. These proteins are present in fish, crustaceans (e.g., shrimp, crab), peanuts, pistachio nuts, sesame seeds, and wheat. To unequivocally establish the likelihood of potential cross-reactivity of the proteins present in the novel food with those established allergens, sera of patients with doctor-diagnosed allergies to these six food categories were screened using ImmunoCAP technology. Of the 106 sera samples tested, 16 showed low IgE binding to Fermotein®. In 11 out of the 16 sera, it was demonstrated by IgE inhibition assays with Proteinase K-digested Fermotein® that all reactivity was directed to fungal carbohydrate moieties. For the remaining five sera, ImmunoCAP inhibition assays with the relevant allergen extracts and with purified human proteins highly homologous to the implicated allergen molecules demonstrated that there was no evidence to support significant cross-reactivity with the potential allergens identified in the bioinformatics in silico search. It is clear that IgE recognition of Fermotein® is dominated by clinically irrelevant carbohydrates. Based on these analyses, it is safe to conclude that Fermotein® presents a negligible allergenicity risk for food-allergic patients because the observed bioinformatics hits did not translate into IgE cross-reactivity.
SN - 2673-6101
ER -