Persistent protective effect of heat-killed Escherichia coli producing “engineered,” recombinant peanut proteins in a murine model of peanut allergy

Li, Xiu Min; Srivastava, Kamal; Grishin, Alexander; Huang, Chih Kang; Schofield, Brian; Burks, Wesley; Sampson, Hugh A.

doi:10.1067/mai.2003.1622

Cited by 181 publications

(126 citation statements)

References 39 publications

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“…It is not easy to eliminate wheat as wheat flour is used in many kinds of cooking, so patients with wheat allergy desire hypoallergic wheat products. Immunotherapy using recombinant-mutated allergen was found to be successful for a peanut allergy in an animal model (42). In combination with the major IgE-binding epitopes of -5 gliadin, the elucidation of major IgE-binding epitopes on HMW-glutenin in this study may provide a useful tool for developing hypoallergenic foods as well as an immunotherapy for patients with WDEIA.…”

Section: Discussionmentioning

confidence: 95%

Specific IgE Determination to Epitope Peptides of ω-5 Gliadin and High Molecular Weight Glutenin Subunit Is a Useful Tool for Diagnosis of Wheat-Dependent Exercise-Induced Anaphylaxis

Matsuo

Kohno

Niihara

et al. 2005

The Journal of Immunology

165

126

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Wheat ω-5 gliadin and a high m.w. glutenin subunit (HMW-glutenin) have been reported as major allergens in wheat-dependent exercise-induced anaphylaxis. A simultaneous detection of specific IgE to epitope sequences of both proteins is considered to be a reliable method for diagnosis of wheat-dependent exercise-induced anaphylaxis. However, the IgE-binding epitope of HMW-glutenin remains unknown. The aim of this study was to determine the IgE-binding epitopes of HMW-glutenin to establish a useful system of identifying patients with wheat-dependent exercise-induced anaphylaxis. For determination of IgE-binding epitopes of HMW-glutenin overlapping peptides were synthesized and reactivities of IgE Abs in the sera of patients to those peptides were analyzed. Three IgE-binding epitopes, QQPGQ, QQPGQGQQ, and QQSGQGQ, were identified within primary sequence of HMW-glutenin. Epitope peptides, which include IgE-binding sequences of ω-5 gliadin and a HMW-glutenin, were synthesized and peptide-specific IgE Abs were measured by CAP-System fluorescent enzyme immunoassay. Twenty-nine of 30 patients with wheat-dependent exercise-induced anaphylaxis had specific IgE Abs to these epitope peptides. None of the 25 sera from healthy subjects reacted to both epitope peptides. Twenty-five patients with atopic dermatitis who had specific IgE to wheat and/or gluten had very low or nonexistent levels of epitope peptide-specific IgE Abs. These results indicated that measurement of IgE levels specific to epitope peptides of ω-5 gliadin and HMW-glutenin is useful as an in vitro diagnostic method for the assessment of patients with wheat-dependent exercise-induced anaphylaxis.

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Section: Discussionmentioning

confidence: 95%

Specific IgE Determination to Epitope Peptides of ω-5 Gliadin and High Molecular Weight Glutenin Subunit Is a Useful Tool for Diagnosis of Wheat-Dependent Exercise-Induced Anaphylaxis

Matsuo

Kohno

Niihara

et al. 2005

The Journal of Immunology

165

126

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“…Modified peanut allergens (Ara h 1, 2, 3), altered using site-directed mutagenesis, can stimulate T cells from peanut-allergic individuals to proliferate, but have greatly reduced IgE-binding capacity as compared with wild-type peanut protein (89). Heat-killed E. coli producing recombinant peanut proteins have demonstrated protective effects in a murine model of peanut anaphylaxis (90). The mechanisms hypothesized to induce this effect include activation of T regulatory cells and downregulation of Th2 cells and reduction of mast cell mediator release on reexposure to antigen (91).…”

Section: Allergen-specific Therapiesmentioning

confidence: 99%

Food allergy

Wang¹,

Sampson²

2011

J. Clin. Invest.

Self Cite

152

117

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Food allergies affect up to 6% of young children and 3%-4% of adults. They encompass a range of disorders that may be IgE and/or non-IgE mediated, including anaphylaxis, pollen food syndrome, food-protein-induced enterocolitis syndrome, food-induced proctocolitis, eosinophilic gastroenteropathies, and atopic dermatitis. Many complex host factors and properties of foods are involved in the development of food allergy. With recent advances in the understanding of how these factors interact, the development of several novel diagnostic and therapeutic strategies is underway and showing promise. Conflict of interest: Hugh A. Sampson is an investor in and paid consultant forAllertein Therapeutics and an investor in Herbal Springs LLC, a holding company for the patents on FAHF-2. Hugh A. Sampson receives research support from the Food Allergy Initiative, a nonprofit foundation supporting food allergy research.

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“…In patients susceptible to shrimp allergies, avoidance is virtually the only way in preventing hypersensitive reactions to shrimp. In the absence of effective treatment modalities in food allergies, appropriate animal models are often needed to investigate the mechanisms of sensitization and immune responses, as well as the possible prophylactic and therapeutic strategies to reduce the allergic responses [17,18,19,20,21,22,23]. Since tropomyosin is the major heat-stable shrimp allergen [14, 16] and accounts for 20% of total protein in shrimp [24], we have used the recombinant protein to elicit a focused hypersensitive response to tropomyosin in mice.…”

Section: Introductionmentioning

confidence: 99%

Induction of Shrimp Tropomyosin-Specific Hypersensitivity in Mice

Leung¹,

Lee²,

Tang³

et al. 2008

Int Arch Allergy Immunol

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Background: Shellfish hypersensitivity is amongst the most common food allergies. The major shellfish allergen was identified as tropomyosin. Here, we investigated the immediate hypersensitivity responses, IgE and cell-mediated immune response in mice sensitized with recombinant shrimp tropomyosin. Methods: Shrimp tropomyosin was cloned and expressed as a His-tagged fusion recombinant protein in Escherichia coli. Three- to 4-week-old BALB/c mice were sensitized by intragastric administration of recombinant tropomyosin (0.1 mg) plus cholera toxin (10 µg) on days 0, 12, 19 and 26 and challenged on day 33. Mice fed with phosphate-buffered saline plus cholera toxin were included as controls. Animals were monitored for immediate hypersensitive responses and tropomyosin-specific IgE over time. In addition, shrimp tropomyosin-specific CD4+ T cells, interleukin-4 and interferon-γ levels were determined from in vitro splenocyte cultures. A passive cutaneous anaphylaxis assay was also conducted. Results: Mice fed with shrimp tropomyosin developed swelling of the snout, increased scratching behavior and shrimp tropomyosin-specific IgE. Sera from tropomyosin-sensitized mice elicited vascular leakage in naïve mice in the passive cutaneous anaphylaxis assay. Shrimp tropomyosin-specific CD4+ T cell proliferations and elevated interleukin-4 over interferon-γ levels were evident in splenocyte cultures of tropomyosin-fed mice upon tropomyosin stimulation. In contrast, shrimp tropomyosin-specific IgE, CD4+ T cells and hypersensitive responses were absent in the control mice. Conclusion: We have generated a BALB/c model of shrimp allergy. This model provides a useful tool for evaluating the immunopathogenic mechanisms involved in shellfish hypersensitivity.

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Persistent protective effect of heat-killed Escherichia coli producing “engineered,” recombinant peanut proteins in a murine model of peanut allergy

Cited by 181 publications

References 39 publications

Specific IgE Determination to Epitope Peptides of ω-5 Gliadin and High Molecular Weight Glutenin Subunit Is a Useful Tool for Diagnosis of Wheat-Dependent Exercise-Induced Anaphylaxis

Specific IgE Determination to Epitope Peptides of ω-5 Gliadin and High Molecular Weight Glutenin Subunit Is a Useful Tool for Diagnosis of Wheat-Dependent Exercise-Induced Anaphylaxis

Food allergy

Induction of Shrimp Tropomyosin-Specific Hypersensitivity in Mice

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