IgG and IgE avidity characteristics of peanut allergic individuals

El-Khouly, Fatima; Lewis, Stuart; Pons, Laurent; Burks, A. Wesley; Hourihane, Jonathan

doi:10.1111/j.1399-3038.2007.00542.x

Cited by 25 publications

(21 citation statements)

References 21 publications

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“…This finding also correlates with the severity of symptoms [46]. It has been shown that the avidity of IgE and IgG antibodies to Ara h 2 was related to the severity of peanut allergy in peanut-allergic patients [47]. This is in agreement with the finding that the affinity of IgE antibodies to allergens is one of the primary factors influencing the sensitivity of histamine release [48,49].…”

Section: Discussionsupporting

confidence: 79%

Sensitization with 7S Globulins from Peanut, Hazelnut, Soy or Pea Induces IgE with Different Biological Activities Which Are Modified by Soy Tolerance

Kroghsbo

Bøgh

Rigby

et al. 2011

Int Arch Allergy Immunol

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Background: It is not known why some foods sensitizing via the gastrointestinal tract are prevalent allergenic foods and others are not. Eating habits, processing, and the food matrix have been suggested to influence the allergenicity of a given food. Factors related to protein structure, such as stability to digestion, have also been suggested. 7S globulins from peanut, hazelnut, soy, and pea were studied to determine whether related proteins would induce a similar sensitization when removed from their ‘normal’ matrix. Methods: Brown Norway rats (soy tolerant or nontolerant) were immunized i.p. 3 times with 100 µg purified peanut, hazelnut, soy, or pea 7S without adjuvant. Sera were analyzed for specific antibodies by different ELISAs (IgG1, IgG2a, and IgE), inhibition ELISA, and rat basophilic leukemia cell assay. Results: The 4 related 7S globulins induced a response with an almost identical level of specific antibodies, but peanut 7S induced IgE of higher avidity than hazelnut and pea 7S which, again, had a higher avidity than IgE induced by soy 7S. Soy tolerance reduced the functionality of IgE without influencing antibody titers. Conclusions: Although the 4 7S globulins are structurally related allergens, they induce antibodies with different antigen-binding characteristics. Peanut 7S induces IgE of a higher avidity than hazelnut and pea 7S which, again, has a higher avidity than IgE induced by soy 7S. We also show that soy tolerance influences the function of antibodies to peanut 7S. These findings may help explain how antibodies of different clinical significances can develop in different individuals sensitized to the same allergen.

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Section: Discussionsupporting

confidence: 79%

Sensitization with 7S Globulins from Peanut, Hazelnut, Soy or Pea Induces IgE with Different Biological Activities Which Are Modified by Soy Tolerance

Kroghsbo

Bøgh

Rigby

et al. 2011

Int Arch Allergy Immunol

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“…Second, allergen-specific IgGs with the capacity to compete for the IgE-binding epitopes might cause invalid effector cell activation, despite the presence of adequate sIgEs [91], [92] and [93] ; a few studies even hint at a high IgE/IgG ratio as a prognostic marker in food allergy, [94] and [95] whereas others did not verify such a correlation. 96 Because IgE versus IgG competition might also interfere with IgE quantifications, novel approaches initially capture all serum IgE at a solid phase and use labeled allergen for the detection of the captured antibodies. 97 Third, qualitative differences of the respective sIgEs might be responsible for uneven efficacy in effector cell activating.…”

Section: Quantification Of Ige Antibodiesmentioning

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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“…Calculations were performed as described by El-Khouly et al [20]. For further description of the basis for this avidity measurement methodology, see El-Khouly et al [20] and Pullen et al [21]. …”

Section: Methodsmentioning

confidence: 99%

“…For measurement of the strength of binding between antigens and IgG1 antibodies a thiocyanate inhibition ELISA based on the method described by El-Khouly et al [20] was conducted. Plates (96 well, Maxisorp, Nunc) were coated with 100 µl/well of 10 µg/ml antigen solution in carbonate buffer and incubated overnight at 4°C.…”

Section: Methodsmentioning

confidence: 99%

The Sensitising Capacity of Intact β-Lactoglobulin Is Reduced by Co-Administration with Digested β-Lactoglobulin

Bøgh

Barkholt

Madsen

2012

Int Arch Allergy Immunol

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Background: It is generally believed that protein hydrolysis in the gastrointestinal tract decreases the allergenicity of food allergens. However, it remains unknown if specific properties of digestion products determine whether a sensitisation or tolerogenic immune response will develop. We sought to examine the sensitising capacity of the cow’s milk allergen β-lactoglobulin (BLG) and digestion products thereof in a Brown Norway (BN) rat model. Methods: Intact BLG was digested in an in vitro model simulating the gastro-duodenal digestion process and subsequently fractionated by gel permeation chromatography. BN rats were dosed with either PBS, 200 µg of intact BLG, 30 µg of intact BLG, 200 µg of partially digested BLG, 200 µg of digested BLG, or with 200 µg of a fraction of large complexes or a fraction of small complexes. Sera from BN rats were analysed for specific antibodies and avidity was measured. Results: BLG partly resisted the digestion process. However, the BLG molecules that did not survive the digestion process were rapidly broken down to peptides of sizes less than M_r 4,500. Specific antibody responses revealed that both 200 and 30 µg of intact BLG had immunogenic as well as sensitising capacity, while digested BLG could not induce any specific antibodies. Most importantly, while intact BLG showed a significant sensitising capacity when administered alone, this sensitising capacity was significantly reduced when co-administered with digested BLG. Conclusions: Co-immunisation of intact BLG with digested BLG reduces the sensitising capacity of intact BLG, which could result from tolerogenic mechanisms induced by the digestion products.

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IgG and IgE avidity characteristics of peanut allergic individuals

Cited by 25 publications

References 21 publications

Sensitization with 7S Globulins from Peanut, Hazelnut, Soy or Pea Induces IgE with Different Biological Activities Which Are Modified by Soy Tolerance

Sensitization with 7S Globulins from Peanut, Hazelnut, Soy or Pea Induces IgE with Different Biological Activities Which Are Modified by Soy Tolerance

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

The Sensitising Capacity of Intact β-Lactoglobulin Is Reduced by Co-Administration with Digested β-Lactoglobulin

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