Allergenic epitopes of bovine ?<sub>S1</sub>-casein recognized by human IgE and IgG

Spuergin, P.; Mueller, H.; Walter, Michael; Schiltz, Emile; Förster, Johannes

doi:10.1111/j.1398-9995.1996.tb00090.x

Cited by 31 publications

(70 citation statements)

References 15 publications

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“…The most frequently recognized ␣S1-casein-derived synthetic peptides were Cas1 and Cas5, which were recognized by IgE Abs of 86.5% and 81.1% of the r␣S1-casein-reactive patients. This finding is in agreement with earlier studies that identified regions covered by Cas1 and Cas5 as major B cell epitopes (18,19,34). Interestingly, Cas3 was recognized also by patients without IgE reactivity to complete r␣S1-casein or the natural ␣-casein fraction, suggesting that this region contains a cryptic epitope that becomes accessible to IgE Abs after digestion of ␣S1-casein.…”

Section: Discussionsupporting

confidence: 82%

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

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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.

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Section: Discussionsupporting

confidence: 82%

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

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“…[10], [120], [121], [122] and [123] [124], [125], [126], [127], [128], [129] and [130] However, other studies at different shifting offsets, with different peptides sizes, or both revealed different sets of immunodominant sequential epitopes for the same allergens. [29], [124], [125], [126], [127], [130] and [131] Nevertheless, approaches to use these alleged immunodominant peptides for the risk assessment of life-threatening symptoms, as well as the prediction of persistence in food hypersensitivity, were apparently successful.…”

Section: Diagnosis Of Food Allergy With Synthetic Sequential Epitopesmentioning

confidence: 99%

“…[29], [124], [125], [126], [127], [130] and [131] Nevertheless, approaches to use these alleged immunodominant peptides for the risk assessment of life-threatening symptoms, as well as the prediction of persistence in food hypersensitivity, were apparently successful. In wheat-dependent exerciseinduced anaphylaxis, all sera from affected patients showed significant sIgE reactivity to the respective peptides, whereas none of the sera from nonatopic control subjects demonstrated reactivity, and sera from control patients with atopic dermatitis showed very low to nonexistent reactivity.…”

Section: Diagnosis Of Food Allergy With Synthetic Sequential Epitopesmentioning

confidence: 99%

Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes

Steckelbroeck¹,

Ballmer‐Weber²,

Vieths³

2008

Journal of Allergy and Clinical Immunology

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This article aims to critically review developments in food allergy diagnostics with regard to the verification of specific IgE antibodies and the identification of the responsible allergens. Results of IgE-binding tests with food extracts are hampered by cross-reactive proteins, low-quality test agents, or both. Specificity can be increased by defining adequate cutoff values, whereas sensitivity can be improved by using high-quality test agents. IgE-binding tests with purified allergens enabled reliable quantification of allergen-specific IgE titers, with higher levels found in individuals with food allergy compared with individuals without food allergy. However, the overlap in individual test reactivity between allergic and nonallergic subjects complicates interpretation. Recombinant allergens and synthetic sequential epitopes enabled detection of sensitization profiles, with IgE specific to several allergens and substructures now being suggested as markers of severity, persistence, or both. However, high-power quantitative studies with larger numbers of patients are required to confirm these markers. This article aims to critically review developments in food allergy diagnostics with regard to the verification of specific IgE antibodies and the identification of the responsible allergens. Results of IgE-binding tests with food extracts are hampered by cross-reactive proteins, low-quality test agents, or both. Specificity can be increased by defining adequate cutoff values, whereas sensitivity can be improved by using high-quality test agents. IgE-binding tests with purified allergens enabled reliable quantification of allergen-specific IgE titers, with higher levels found in individuals with food allergy compared with individuals without food allergy. However, the overlap in individual test reactivity between allergic and nonallergic subjects complicates interpretation. Recombinant allergens and synthetic sequential epitopes enabled detection of sensitization profiles, with IgE specific to several allergens and substructures now being suggested as markers of severity, persistence, or both.However, high-power quantitative studies with larger numbers of patients are required to confirm these markers. IgE-mediated and non-IgE-mediated syndromes, where IgE-mediated manifestations are responsible for the majority of food-induced, immediate-type, immune-mediated hypersensitivity reactions. 3 The development of an IgE-mediated response to food requires a series of molecular and cellular interactions, which involve antigenpresenting cells, T lymphocytes, and B lymphocytes. [4] and [5] Depending on the route of sensitization, food allergy is the result of either genuine reactivity to comestibles through the gastrointestinal tract (class I food allergens) or secondary sensitization to cross-reactive food allergens as a consequence of the initial reactivity to homologous pollen-related allergens (class II food allergens). [6] and [7] The majority of class I food allergens are heat stable and resistan...

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“…Caseins and b-lactoglobulin (b-Lg) have been described as the main antigenic and allergenic components for human beings [3,4], although immunoglobulins, a-lactalbumin (a-La), and bovine serum albumin (BSA) were also found to be reactive with different isotypes of human antibodies [5,6]. Several immunoreactive epitopes have been identified in caseins [7,8] and b-Lg [9]. Most of the epitopes present in the casein molecules are sequential since the high number of proline and hydrophobic residues (45%) in these proteins determine an undefined secondary and tertiary structure [10].…”

Section: Introductionmentioning

confidence: 99%

Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk

Rozenfeld

Docena

Añón

et al. 2002

Clinical and Experimental Immunology

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Food allergy is becoming a medical, economical and social problem. Soybean, together with milk, peanuts and eggs, are the major allergenic foods. This pathology affects the infant population, when the gut barrier is immature and the immune system is still refining its ability to tolerate food proteins. In our country, cow's milk allergy (CMA) constitutes the main food allergy in infancy, but soy allergy has become exacerbated because of the increased utilization of soy-based formulas as cow's milk (CM) substitutes and the inclusion of soy-proteins in many processed foods. Once a food allergy is diagnosed, the only proven therapy is the strict elimination of the offending allergens from the diet. Available substitutes for CM include milks from different mammalian animals, soy-based formulas, hydrolysed cow's milk proteins (CMP) and amino acid-based formulas. Furthermore, there is evidence that soy proteins may trigger allergic reactions in CMA patients, as assessed by a double-blind placebo controlled food challenge (DBPCFC) [1].Milk contains more than 50 proteins and the major ones are implicated in a number of immunologically mediated reactions [2]. Caseins and b-lactoglobulin (b-Lg) have been described as the main antigenic and allergenic components for human beings [3,4], although immunoglobulins, a-lactalbumin (a-La), and bovine serum albumin (BSA) were also found to be reactive with different isotypes of human antibodies [5,6]. Several immunoreactive epitopes have been identified in caseins [7,. Most of the epitopes present in the casein molecules are sequential since the high number of proline and hydrophobic residues (45%) in these proteins determine an undefined secondary and tertiary structure [10]. Besides, caseins tend to aggregate as a result of hydrophobic interactions to give quaternary structures [11], and this may create conformational epitopes buried in the hydrophobic interior of the micelle [7]. These epitopes are only exposed and accessible to the immune system after denaturation of the complex by digestion.A number of soy proteins that bind antibodies, especially IgE, have been identified [12,13]. The main fractions of storage globulins from seed proteins are the complexes 7S or b-conglycinin, and 11S or glycinin. The 7S complex is generally a trimer with MW 150-200 kD, whereas 11S is a hexamer with MW 300-400 kD [14]. In the 7S fraction, or b-conglycinin, several IgE-binding proteins have been identified and some of them have been purified and characterized: Gly m Bd 28K, Gly m Bd 30K, Gly m Bd 60K [15,16]. Sequence homology has been reported between these allergens and the thiol proteinase family SUMMARYSoy-based formulas are the most employed cow's milk substitutes in the treatment of cow's milk allergy in our country. Since adverse reactions have been reported in allergic patients as a consequence of exposure to soy proteins, we have investigated the possible cross-reactivity between components from soybean and cow's milk. A cow's milk specific polyclonal antiserum and casein specific m...

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Allergenic epitopes of bovine ?_S1-casein recognized by human IgE and IgG

Cited by 31 publications

References 15 publications

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

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

Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes

Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk

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Allergenic epitopes of bovine ?S1-casein recognized by human IgE and IgG

Cited by 31 publications

References 15 publications

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

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

Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes

Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk

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Product

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Allergenic epitopes of bovine ?_S1-casein recognized by human IgE and IgG