title: The lipid interaction capacity of Sin a 2 and Ara h 1, major mustard and peanut allergens of the cupin superfamily, endorses allergenicity.
abstract: Sin a 2 (11S globulin) and Ara h 1 (7S globulin) are major allergens from yellow mustard seeds and peanut, respectively. The ability of these two allergens to interact with lipid components remains unknown.
  
  
  
  To study the capacity of Sin a 2 and Ara h 1 to interact with lipid components and the potential effects of such interaction in their allergenic capacity.
  
  
  
  Spectroscopic and SDS-PAGE binding assays of Sin a 2 and Ara h 1 with different phospholipid vesicles and gastrointestinal and endolysosomal digestions in the presence or absence of lipids were performed. The capacity of human monocyte-derived dendritic cells (hmoDCs) to capture food allergens in the presence or absence of lipids, the induced cytokine signature, and the effect of allergens and lipids to regulate TLR2-L-induced NF-kB/AP-1 activation in THP1 cells were analyzed.
  
  
  
  Sin a 2 and Ara h 1 bind phosphatidylglycerol (PG) acid but not phosphatidylcholine (PC) vesicles in a pH-dependent manner. The interaction of these two allergens with lipid components confers resistance to gastrointestinal digestion, reduces their uptake by hmoDCs, and enhances their stability to microsomal degradation. Mustard and peanut lipids favor a proinflammatory environment by increasing the IL-4/IL-10 ratio and IL-1β production by hmoDCs. The presence of mustard lipids and PG vesicles inhibits TLR2-L-induced NF-kB/AP-1 activation in THP1 cells.
  
  
  
  Sin a 2 and Ara h 1 interact with lipid components, which might well contribute to explain the potent allergenic capacity of these two clinically relevant allergens belonging to the cupin superfamily.
authors.affiliation: Department of Biochemistry and Molecular Biology, School of Chemistry, Complutense University of Madrid, Madrid, Spain.
authors.forename: A
authors.initials: A
authors.lastname: Angelina
authors.affiliation: Department of Biochemistry and Molecular Biology, School of Chemistry, Complutense University of Madrid, Madrid, Spain.
authors.forename: S
authors.initials: S
authors.lastname: Sirvent
authors.affiliation: Department of Pathophysiology and Allergy Research, Medical University of Vienna, Vienna, Austria.
authors.forename: C
authors.initials: C
authors.lastname: Palladino
authors.affiliation: Servicio de Alergia, Fundación Jiménez Diaz, Madrid, Spain.
authors.forename: A
authors.initials: A
authors.lastname: Vereda
authors.affiliation: Servicio de Alergia, Fundación Jiménez Diaz, Madrid, Spain.
authors.forename: J
authors.initials: J
authors.lastname: Cuesta-Herranz
authors.affiliation: Department of Paediatrics and Adolescent Medicine, Medical University of Vienna, Vienna, Austria.|Division of Immunology and Allergy, Food allergy and Anaphylaxis Program, The Department of Paediatrics, Hospital for Sick Children, The University of Toronto, Toronto, ON, Canada.
authors.forename: T
authors.initials: T
authors.lastname: Eiwegger
authors.affiliation: Department of Biochemistry and Molecular Biology, School of Chemistry, Complutense University of Madrid, Madrid, Spain.
authors.forename: R
authors.initials: R
authors.lastname: Rodríguez
authors.affiliation: Department of Pathophysiology and Allergy Research, Medical University of Vienna, Vienna, Austria.
authors.forename: H
authors.initials: H
authors.lastname: Breiteneder
authors.affiliation: Department of Biochemistry and Molecular Biology, School of Chemistry, Complutense University of Madrid, Madrid, Spain.
authors.forename: M
authors.initials: M
authors.lastname: Villalba
authors.affiliation: Department of Biochemistry and Molecular Biology, School of Chemistry, Complutense University of Madrid, Madrid, Spain.
authors.forename: O
authors.initials: O
authors.lastname: Palomares
mesh_terms: D000485:Allergens / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism; D052179:Antigens, Plant / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism; D016207:Cytokines / Q000378:metabolism; D022162:Cytoplasmic Vesicles / Q000378:metabolism; D003713:Dendritic Cells / Q000276:immunology / Q000378:metabolism; D011992:Endosomes / Q000378:metabolism; D005512:Food Hypersensitivity / Q000276:immunology* / Q000378:metabolism*; D006023:Glycoproteins / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology; D008055:Lipids; D008247:Lysosomes / Q000378:metabolism; D008565:Membrane Proteins; D008958:Models, Molecular; D016328:NF-kappa B / Q000378:metabolism; D021183:Peanut Hypersensitivity / Q000276:immunology / Q000378:metabolism; D010715:Phosphatidylglycerols / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism; D011487:Protein Conformation; D059748:Proteolysis; D051195:Toll-Like Receptor 2 / Q000378:metabolism
chemical_list: D000485:Allergens; D052179:Antigens, Plant; C500889:Ara h 1 protein, Arachis hypogaea; D016207:Cytokines; D006023:Glycoproteins; D008055:Lipids; D008565:Membrane Proteins; D016328:NF-kappa B; D010715:Phosphatidylglycerols; D010940:Plant Proteins; C512826:Sin a 2 protein, Sinapis alba; D051195:Toll-Like Receptor 2; D007073:Immunoglobulin E
keywords: 11S and 7S globulins; allergens; dendritic cells; food allergy; lipid-binding capacity