ArticleAnnals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology2023
High prevalence of lupin allergy among patients with peanut allergy: Identification of γ-conglutin as major allergen.
Article in Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Food-induced anaphylaxis to plant allergens in adolescents and adults: Data from the allergy Vigilance Network (2002-2024).The World Allergy Organization journal · 2026Article
- What Makes Lupins Less Palatable to Consumers? Can the Sensory Quality of Lupin be Improved and Commercialized?Comprehensive reviews in food science and food safety · 2025Review
- IgE-Mediated Legume Allergy: A Pediatric Perspective.Journal of personalized medicine · 2024Review
- γ-Conglutin Immunoreactivity Is Differently Affected by Thermal Treatment and Gastrointestinal Digestion in Lupine Species.Foods (Basel, Switzerland) · 2024Article
- Influence of Roasting Temperature on the Detectability of Potentially Allergenic Lupin by SDS-PAGE, ELISAs, LC-MS/MS, and Real-Time PCR.Foods (Basel, Switzerland) · 2024Article
- Lupin allergy: Another member of the peanut gallery?Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology · 2023Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLupin is a protein-rich legume with a growing presence in the food market worldwide. With increased consumption, lupin allergy (LA) reports are also rising. Uncertainties exist on the cross-reactivity between peanut and lupin, the allergenic potential of different lupin species, and sensitization patterns among different populations.
objectiveTo evaluate the molecular basis of LA and to determine lupin allergens from 3 different species that may be involved in peanut allergy (PA) cross-reactivity.
methodsA total of 43 subjects with PA, those with LA, or controls without food allergy were evaluated with skin prick tests (SPTs) and specific IgEs (sIgEs). Lupin-sensitized subjects were offered a lupin oral food challenge (OFC). Immunoblots and enzyme-linked immunosorbent assays were performed on sera from lupin-sensitized subjects.
resultsIn this study, 44% of the PA subjects were confirmed to have LA by OFC. Anaphylaxis was the most frequent manifestation after lupin consumption, with a minimal eliciting dosage of 1 g lupin flour. There was no difference in lupin sIgE or SPT wheal size between lupin-sensitized and confirmed LA subjects or in the severity of symptoms among confirmed LA subjects. Sera from lupin-sensitized subjects uniformly reacted to all 3 different lupin species. Immunoblotting and enzyme-linked immunosorbent assays revealed immunoglobulin E binding to α- and γ-conglutin in all analyzed sera, whereas α- and β-conglutin recognition was variable.
conclusionOur findings reveal a high prevalence of LA among PA subjects, emphasizing lupin must be labeled as an allergen in foods. Owing to high variability in lupin-sIgE and lupin-SPT results, LA diagnosis may require OFC. In our population, γ-conglutin is the major allergen of lupin.
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