Mediator release assays based on human or murine immunoglobulin E in allergen standardization

Kaul, Susanne; Lüttkopf, D.; Kastner, B.; Vogel, Lothar; Höltz, G.; Vieths, Stefan; Hoffmann, Andreas

doi:10.1111/j.1365-2222.2006.02618.x

Cited by 57 publications

(56 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…RBL cells (clone RBL-703/21) transfected with the human FcεRI (28) were incubated with sera (diluted 1:20) from two wheat food-allergic patients (nos. 19 and 22) who showed positive dot blot results to rTri a 36 or with serum from grass pollen-allergic patients without wheat food allergy.…”

Section: Basophil Activation Assaysmentioning

confidence: 99%

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Baar

Pahr

Constantin

et al. 2012

The Journal of Immunology

View full text Add to dashboard Cite

Wheat is an essential element in our nutrition but one of the most important food allergen sources. Wheat allergic patients often suffer from severe gastrointestinal and systemic allergic reactions after wheat ingestion. In this study, we report the molecular and immunological characterization of a new major wheat food allergen, Tri a 36. The cDNA coding for a C-terminal fragment of Tri a 36 was isolated by screening a wheat seed cDNA expression library with serum IgE from wheat food-allergic patients. Tri a 36 is a 369-aa protein with a hydrophobic 25-aa N-terminal leader peptide. According to sequence comparison it belongs to the low m.w. glutenin subunits, which can be found in a variety of cereals. The mature allergen contains an N-terminal domain, a repetitive domain that is rich in glutamine and proline residues, and three C-terminal domains with eight cysteine residues contributing to intra- and intermolecular disulfide bonds. Recombinant Tri a 36 was expressed in Escherichia coli and purified as soluble protein. It reacted with IgE Abs of ∼80% of wheat food-allergic patients, showed IgE cross-reactivity with related allergens in rye, barley, oat, spelt, and rice, and induced specific and dose-dependent basophil activation. Even after extensive in vitro gastric and duodenal digestion, Tri a 36 released distinct IgE-reactive fragments and was highly resistant against boiling. Thus, recombinant Tri a 36 is a major wheat food allergen that can be used for the molecular diagnosis of, and for the development of specific immunotherapy strategies against, wheat food allergy.

show abstract

Section: Basophil Activation Assaysmentioning

confidence: 99%

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Baar

Pahr

Constantin

et al. 2012

The Journal of Immunology

View full text Add to dashboard Cite

show abstract

“…RBL cells (clone RBL-703/21) transfected with the human FcRI receptor (29) were cultured in RPMI 1640 medium supplemented with 10% FCS, 4 mM L-glutamine, 2 mM sodium pyruvate, 10 mM HEPES, 100 M 2-ME, and 1% penicillin/streptomycin. Cells were resuspended in culture medium (2 ϫ 10 6 cells/ml), and 50 l of this solution per well of a 96-well flat bottom microplate was pipetted.…”

Section: Rbl Assaysmentioning

confidence: 99%

Cloning, Expression, and Mapping of Allergenic Determinants of αS1-Casein, a Major Cow’s Milk Allergen

Schulmeister¹,

Hochwallner²,

Swoboda

et al. 2009

The Journal of Immunology

View full text Add to dashboard Cite

Milk is one of the first components introduced into human diet. It also represents one of the first allergen sources, which induces IgE-mediated allergies in childhood ranging from gastrointestinal, skin, and respiratory manifestations to severe life-threatening manifestations, such as anaphylaxis. Here we isolated a cDNA coding for a major cow’s milk allergen, αS1-casein, from a bovine mammary gland cDNA library with allergic patients’ IgE Abs. Recombinant αS1-casein was expressed in Escherichia coli, purified, and characterized by circular dichroism as a folded protein. IgE epitopes of αS1-casein were determined with recombinant fragments and synthetic peptides spanning the αS1-casein sequence using microarrayed components and sera from 66 cow’s milk-sensitized patients. The allergenic activity of rαS1-casein and the αS1-casein-derived peptides was determined using rat basophil leukemia cells transfected with human FcεRI, which had been loaded with the patients’ serum IgE. Our results demonstrate that rαS1-casein as well as αS1-casein-derived peptides exhibit IgE reactivity, but mainly the intact rαS1-casein induced strong basophil degranulation. These results suggest that primarily intact αS1-casein or larger IgE-reactive portions thereof are responsible for IgE-mediated symptoms of food allergy. Recombinant αS1-casein as well as αS1-casein-derived peptides may be used in clinical studies to further explore pathomechanisms of food allergy as well as for the development of new diagnostic and therapeutic strategies for milk allergy.

show abstract

“…As a matter of fact, a high content of polyphenols in the matrix (as in the case of red wines) could generate interactions both with proteins and antibodies (Weber et al 2007b). Moreover, in these immunological tests, also the adsorption to solid matrices of the allergens could alter epitopes (Kaul et al 2007) compromising the reaction sensitivity in relation to the antibodies used.…”

Section: Reviewmentioning

confidence: 99%

“…The high sensitivity, accuracy, and reproducibility of the MS techniques (Picariello et al 2011) allow the detection of trace amounts of proteins and make the identification independent of the protein structure (Kaul et al 2007;Kirsch et al 2009).…”

Section: Reviewmentioning

confidence: 99%

Hidden exogenous proteins in wine: problems, methods of detection and related legislation - a review

Rizzi¹,

Mainente²,

Pasini³

et al. 2016

Czech J. Food Sci.

View full text Add to dashboard Cite

Rizzi C., Mainente F., Pasini G., Simonato B. (2016): Hidden exogenous proteins in wine: problems, methods of detection and related legislation -a review. Czech J. Food Sci., 34: 93-104.Fining agents are commonly used in the winemaking process to clarify and stabilise wines. They have different origins (animal, vegetal or mineral) and are added to wines in order to remove specifically undesirable compounds that are discarded. Fining agents should not be present in the final product but their possible persistence, as well as other exogenous residual proteins such as the enzymes utilised in winemaking, cannot be excluded for sure. The principal concern about the presence of exogenous residual proteins is the health of allergic subjects. Nevertheless, the respect of religious creed or other practice of living of the consumer must be considered as well. In the present review we itemise the proteins used in winemaking and possible drawbacks of their permanence in the final products and the related risks, depict the status of the art of the studies performed about the detection of exogenous proteins, and describe the wine labelling laws adopted in different countries to avoid the drawbacks associated with these hidden substances.

show abstract

Mediator release assays based on human or murine immunoglobulin E in allergen standardization

Cited by 57 publications

References 33 publications

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Cloning, Expression, and Mapping of Allergenic Determinants of αS1-Casein, a Major Cow’s Milk Allergen

Hidden exogenous proteins in wine: problems, methods of detection and related legislation - a review

Contact Info

Product

Resources

About