Studies of hypersensitivity reactions to foods in infants and children

Sa, Bock; Wy, Lee; Lk, Remigio; Cd, May

doi:10.1016/0091-6749(78)90132-x

Cited by 294 publications

(100 citation statements)

References 5 publications

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“…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.…”

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confidence: 99%

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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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mentioning

confidence: 99%

“…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.…”

mentioning

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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“…1,2 The clinical features of peanut allergy (PNA) are frequently expressed as acute IgE-mediated reactions after ingestion of peanuts. [3][4][5][6][7][8] Peanuts and tree nuts together account for the majority of fatal and near-fatal, food-induced, anaphylactic reactions in the United States. 3 The prevalence of PNA has increased in the past decades 8 and now affects about 1.5 million Americans.…”

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confidence: 99%

A murine model of peanut anaphylaxis: T- and B-cell responses to a major peanut allergen mimic human responses

Li¹,

Serebrisky²,

Lee³

et al. 2000

Journal of Allergy and Clinical Immunology

397

377

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Background: Peanut allergy affects 0.6% of the US population. At the present time, allergen avoidance is the only therapeutic option. Animal models of food-induced anaphylaxis would facilitate attempts to design novel immunotherapeutic strategies for the treatment of peanut allergy. Objective: The purpose of this study was to develop a murine model of IgE-mediated peanut hypersensitivity that closely mimics human peanut allergy. Methods: C3H/HeJ mice sensitized orally with freshly ground whole peanut and cholera toxin as adjuvant were challenged orally 3 and 5 weeks later with crude peanut extract. Anaphylactic reactions were determined. T-and B-cell responses to Ara h 1 and Ara h 2, the major peanut allergens, were characterized by evaluating splenocyte proliferative responses and IgE antibody concentrations. Furthermore, IgE antibodies in the sera of patients with peanut allergy and mice were compared for antibody binding to Ara h 2 isoforms and allergenic epitopes. Results: Peanut-specific IgE was induced by oral peanut sensitization, and hypersensitivity reactions were provoked by feeding peanut to sensitized mice. The symptoms were similar to those seen in human subjects. Ara h 1-and Ara h 2-specific antibodies were present in the sera of mice with peanut allergy. Furthermore, these Ara h 2-specific IgE antibodies bound the same Ara h 2 isoforms and major allergenic epitopes as antibodies in the sera of human subjects with peanut allergy.

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“…In a controlled setting with experienced clinicians, the DBPCFC can be safely performed (Bock et al 1978(Bock et al , 1988Watson 1995;Williams and Bock 1999). The rapidity of IgE-mediated reactions (> 90% within 1 hr) allows the DBPCFC to reproduce objectively IgEmediated symptoms resulting from the food administered.…”

Section: Use Of Human Clinical Datamentioning

confidence: 99%

“…Interpretation of the usefulness of SPT or food-specific IgE rests with the comparison of SPT/specific IgE results with the outcome of double-blind, placebo-controlled food challenge (DBPCFC), which is currently the "gold standard" for determining food allergy. Approximately 50% of positive SPTs correlate with confirmed DBPCFCs, suggesting that sensitization to food allergens occurs in the absence of clinical symptoms (Bock et al 1977(Bock et al , 1978Eigenmann and Sampson 1998). The magnitude of the SPT or specific IgE measurement is useful in predicting the likelihood of clinical allergy (as confirmed by DBPCFC) but is not useful in predicting severity (Eigenmann and Sampson 1998;Sampson 2001).…”

Section: Use Of Human Clinical Datamentioning

confidence: 99%

Key issues for the assessment of the allergenic potential of genetically modified foods: breakout group reports.

Germolec

Kimber

Goldman

et al. 2003

Environ Health Perspect

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On the final afternoon of the workshop "Assessment of the Allergenic Potential of Genetically Modified Foods," held 10-12 December 2001 in Chapel Hill, North Carolina, USA, speakers and participants met in breakout groups to discuss specific questions in the areas of use of human clinical data, animal models to assess food allergy, biomarkers of exposure and effect, sensitive populations, dose-response assessment, and postmarket surveillance. Each group addressed general questions regarding allergenicity of genetically modified foods and specific questions for each subject area. This article is a brief summary of the discussions of each of the six breakout groups regarding our current state of knowledge and what information is needed to advance the field.

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Studies of hypersensitivity reactions to foods in infants and children

Cited by 294 publications

References 5 publications

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

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

A murine model of peanut anaphylaxis: T- and B-cell responses to a major peanut allergen mimic human responses

Key issues for the assessment of the allergenic potential of genetically modified foods: breakout group reports.

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