Proteomic analysis of lupin seed proteins to identify conglutin β as an allergen, Lup an 1

Danica Goggin; G. Mir; Wendy-Anne Smith; M. Stuckey; P.M.C. Smith

doi:10.1021/jf800840u

Proteomic analysis of lupin seed proteins to identify conglutin β as an allergen, Lup an 1

Danica Goggin, G. Mir, Wendy-Anne Smith, M. Stuckey, P.M.C. Smith

Research output: Contribution to journal › Article › peer-review

82 Citations (Scopus)

Abstract

Lupin products may be valuable as human foods because of their high protein content and potential anticholesterolemic properties. However, a small percentage of the population is allergic to lupin. In this study, we use in vitro IgE binding and mass spectrometry to identify conglutin beta, a major storage protein, as an allergen in seeds of Lupinus angustifolius and Lupinus albus. Purification of conglutin beta from L. angustifolius flour confirmed that serum IgE binds to this protein. Where IgE in sera recognized lupin proteins on Western blots, it recognized conglutin beta, suggesting this protein is a major allergen for lupin. The L. angustifolius conglutin beta allergen has been designated Lup an 1 by the International Union of Immunological Societies (IUIS) allergen nomenclature subcommittee.

Original language	English
Pages (from-to)	6370-6377
Journal	Journal of Agricultural and Food Chemistry
Volume	56
Issue number	15
DOIs	https://doi.org/10.1021/jf800840u
Publication status	Published - 2008

Access to Document

10.1021/jf800840u

Cite this

@article{ba99036fcecd42b89444e2e751c96dda,

title = "Proteomic analysis of lupin seed proteins to identify conglutin β as an allergen, Lup an 1",

abstract = "Lupin products may be valuable as human foods because of their high protein content and potential anticholesterolemic properties. However, a small percentage of the population is allergic to lupin. In this study, we use in vitro IgE binding and mass spectrometry to identify conglutin beta, a major storage protein, as an allergen in seeds of Lupinus angustifolius and Lupinus albus. Purification of conglutin beta from L. angustifolius flour confirmed that serum IgE binds to this protein. Where IgE in sera recognized lupin proteins on Western blots, it recognized conglutin beta, suggesting this protein is a major allergen for lupin. The L. angustifolius conglutin beta allergen has been designated Lup an 1 by the International Union of Immunological Societies (IUIS) allergen nomenclature subcommittee.",

author = "Danica Goggin and G. Mir and Wendy-Anne Smith and M. Stuckey and P.M.C. Smith",

year = "2008",

doi = "10.1021/jf800840u",

language = "English",

volume = "56",

pages = "6370--6377",

journal = "Journal of Agricultural and Food Chemistry",

issn = "0021-8561",

publisher = "American Chemical Society",

number = "15",

}

TY - JOUR

T1 - Proteomic analysis of lupin seed proteins to identify conglutin β as an allergen, Lup an 1

AU - Goggin, Danica

AU - Mir, G.

AU - Smith, Wendy-Anne

AU - Stuckey, M.

AU - Smith, P.M.C.

PY - 2008

Y1 - 2008

N2 - Lupin products may be valuable as human foods because of their high protein content and potential anticholesterolemic properties. However, a small percentage of the population is allergic to lupin. In this study, we use in vitro IgE binding and mass spectrometry to identify conglutin beta, a major storage protein, as an allergen in seeds of Lupinus angustifolius and Lupinus albus. Purification of conglutin beta from L. angustifolius flour confirmed that serum IgE binds to this protein. Where IgE in sera recognized lupin proteins on Western blots, it recognized conglutin beta, suggesting this protein is a major allergen for lupin. The L. angustifolius conglutin beta allergen has been designated Lup an 1 by the International Union of Immunological Societies (IUIS) allergen nomenclature subcommittee.

AB - Lupin products may be valuable as human foods because of their high protein content and potential anticholesterolemic properties. However, a small percentage of the population is allergic to lupin. In this study, we use in vitro IgE binding and mass spectrometry to identify conglutin beta, a major storage protein, as an allergen in seeds of Lupinus angustifolius and Lupinus albus. Purification of conglutin beta from L. angustifolius flour confirmed that serum IgE binds to this protein. Where IgE in sera recognized lupin proteins on Western blots, it recognized conglutin beta, suggesting this protein is a major allergen for lupin. The L. angustifolius conglutin beta allergen has been designated Lup an 1 by the International Union of Immunological Societies (IUIS) allergen nomenclature subcommittee.

U2 - 10.1021/jf800840u

DO - 10.1021/jf800840u

M3 - Article

C2 - 18620408

SN - 0021-8561

VL - 56

SP - 6370

EP - 6377

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

IS - 15

ER -

Proteomic analysis of lupin seed proteins to identify conglutin β as an allergen, Lup an 1

Abstract

Access to Document

Fingerprint

Cite this