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Plant protein families and their relationships to food allergy
Abstract
The analysis of plant proteins has a long and distinguished history, with work dating back over 250 years. Much of the work has focused on seed proteins, which are important in animal nutrition and food processing. Early studies classified plant proteins into groups based on solubility ('Osborne fractions') or protein function. More recently, families have been defined based on stuctural and evolutionary relationships. One of the most widespread groups of plant proteins is the prolaminin superfamily, which comprises cereal seed storage proteins, a range of low-molecular-mass sulphur-rich proteins (many of which are located in seeds) and some cell wall glycoproteins. This superfamily includes several major types of plant allergen: non-specific lipid transfer proteins, cereal seed inhibitors of alpha-amylase and/or trypsin, and 2 S albumin storage proteins of dicotyledonous seeds.
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Over 50% of plant protein allergens fall into the prolamin and cupin superfamilies.
“Over 50% of the plant protein allergens fall into two categories, the prolamin and cupin superfamilies [181].”
From Plant Proteins: Assessing Their Nutritional Quality and Effects on Health and Physical Function (2020) · cites this paper as [181]
The prolamin superfamily currently forms the largest and most widely distributed group of plant food allergens.
“Consequently, the prolamin superfamily currently forms the largest and most widely distributed group of plant food allergens [181].”
From Plant Proteins: Assessing Their Nutritional Quality and Effects on Health and Physical Function (2020) · cites this paper as [181]
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Metadata
- Authors
- Shewry, P. R., Beaudoin, F., Jenkins, J., Griffiths-Jones, S., & Mills, E. N. C.
- Affiliations
- University of Bristol (GB)
- Norwich Research Park (GB)
- The Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 ISA, U.K.
- Corresponding author
- Beaudoin, F.
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2002-11-01
- Volume
- 30
- Issue
- 6
- Pages
- 906-910
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W2127038205
- Cited by
- 110
- References
- 2
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 8 · 2023: 6 · 2022: 6 · 2021: 5 · 2020: 4 · 2019: 5 · 2018: 2 · 2017: 1 · 2016: 5 · 2015: 3 · 2014: 3 · 2013: 5 · 2012: 3
- FWCI
- 2.66
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (publishedVersion)
- Rothamsted Repository (Rothamsted Repository) (submittedVersion)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Food Allergy and Anaphylaxis Research
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Health Sciences › Medicine › Immunology and Allergy › Allergic Rhinitis and Sensitization
- Keywords
- plant proteins, food allergy, plant allergens, seed storage proteins, lipid transfer proteins, alpha-amylase inhibitors, trypsin inhibitor, 2S albumin, protein families, protein evolution, cell wall glycoproteins
- MeSH terms
- Animals, Food Hypersensitivity, Humans, Models, Molecular, Phylogeny, Plant Proteins, Plants, Protein Structure, Secondary, Prolamins
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