ArticleNutrients2017
Hypoallergenic Variant of the Major Egg White Allergen Gal d 1 Produced by Disruption of Cysteine Bridges.
Article in Nutrients, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Allergenicity Assessment of Precision Fermentation-Derived Food Proteins.Foods (Basel, Switzerland) · 2026Review
- Meat allergy: Specific reactions to chicken, beef, pork, and alternative protein sources.Asia Pacific allergy · 2026Review
- Genome Editing in the Chicken: From PGC-Mediated Germline Transmission to Advanced Applications.International journal of molecular sciences · 2025Review
- Food Allergens: When Friends Become Foes-Caveats and Opportunities for Oral Immunotherapy Based on Deactivation Methods.Nutrients · 2023Review
- Nematode surface functionalization with hydrogel sheaths tailoredMaterials today. Bio · 2022Article
- Aptamer-Based Fluorescent Biosensor for the Rapid and Sensitive Detection of Allergens in Food Matrices.Foods (Basel, Switzerland) · 2021Review
- Egg Allergy: Diagnosis and Immunotherapy.International journal of molecular sciences · 2020Review
- New Perspectives in Food Allergy.International journal of molecular sciences · 2020Review
- Review
- Potential benefits of gene editing for the future of poultry farming.Transgenic research · 2019Article
- Innovative approaches to genome editing in avian species.Journal of animal science and biotechnology · 2018Review
- Update on oral immunotherapy for egg allergy.Human vaccines & immunotherapeutics · 2017Review
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundGal d 1 (ovomucoid) is the dominant allergen in the chicken egg white. Hypoallergenic variants of this allergen can be used in immunotherapy as an egg allergy treatment approach. We hypothesised that disruption of two of the nine cysteine-cysteine bridges by site-directed mutagenesis will allow the production of a hypoallergenic variant of the protein; Methods: Two cysteine residues at C192 and C210 in domain III of the protein were mutated to alanine using site-directed mutagenesis, to disrupt two separate cysteine-cysteine bridges. The mutated and non-mutated proteins were expressed in
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Registered trials
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