Porcine IgE in the context of experimental food allergy: Purification and isotype-specific antibodies

Rupa, Prithy; Hamilton, Korinne; Cirinna, Melissa; Wilkie, B.N.

doi:10.1016/j.vetimm.2008.05.028

Cited by 19 publications

(13 citation statements)

References 26 publications

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“…Egg white, PN, and whey proteins were all in-house-extracted and partially purified according to methods previously described. − Maillard reaction or glycation was performed as described in a previously established method with slight modifications . In brief, mannose (Sigma-Aldrich, St. Louis, MO, USA) was added to the three proteins at a ratio of 1:1 (w/w protein/mannose), mixed into a solution, freeze-dried, and incubated at 55 °C for 3 days (72 h) at 65% relative humidity using saturated potassium iodide solution in a laboratory incubator.…”

Section: Methodsmentioning

confidence: 99%

Attenuation of Allergic Immune Response Phenotype by Mannosylated Egg White in Orally Induced Allergy in Balb/c Mice

Rupa

Nakamura

Katayama

et al. 2014

J. Agric. Food Chem.

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Food allergies are attributed to an imbalance in immune response to ubiquitous antigens. A previous study demonstrated that mannose glycation (mannosylation) of ovalbumin decreased allergenicity in vivo. The proposed research targets mannosylation of various common allergens that may help prevent food allergy. Balb/c mice (n = 8) were sensitized toxin egg white, peanut, and whey and treated with mannosylated forms of the test antigens. Glucosylated peanut and cholera toxins were used as controls. Allergic status was assessed as clinical signs, serum histamine, mouse mast cell protease (MMCP), antibody activity, cytokines, and T regulatory cells (T-regs). Significant preventative effects were observed with mannosylated egg white treatment such as reduced clinical signs, histamine, MMCP, specific G, G1, and E antibody activities, and IL-4 and increased IL-10 and CD25(+) Foxp3(+) cells. Other groups did not differ significantly. It was concluded that mannosylated egg white provides a powerful tool to prevent allergic phenotypes with possible relevance to control human egg allergy.

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Section: Methodsmentioning

confidence: 99%

Attenuation of Allergic Immune Response Phenotype by Mannosylated Egg White in Orally Induced Allergy in Balb/c Mice

Rupa

Nakamura

Katayama

et al. 2014

J. Agric. Food Chem.

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“…91 In pigs, IgE-mediated allergy and anaphylaxis can be induced experimentally with egg proteins, 72 and most often Gal d 1 was used as antigen. 92,93 In dogs, no significant differences were found between normal and atopic dogs for anti-egg IgG. However, dogs with skin disease had significantly more IgE antibodies to egg and many other antigens than normal dogs.…”

Section: Eggmentioning

confidence: 94%

“…Gal d 1 is an established diagnostic marker in humans . In pigs, IgE‐mediated allergy and anaphylaxis can be induced experimentally with egg proteins, and most often Gal d 1 was used as antigen . In dogs, no significant differences were found between normal and atopic dogs for anti‐egg IgG.…”

Section: Allergen Sources and Moleculesmentioning

confidence: 99%

Comparing immediate‐type food allergy in humans and companion animals—revealing unmet needs

Pali‐Schöll

Lucia²,

Jackson³

et al. 2017

Allergy

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Adverse food reactions occur in human as well as veterinary patients. Systematic comparison may lead to improved recommendations for prevention and treatment in both. In this position paper, we summarize the current knowledge on immediate-type food allergy vs other food adverse reactions in companion animals, and compare this to the human situation. While the prevalence of food allergy in humans has been well studied for some allergens, this remains to be investigated for animal patients, where owner-reported as well as veterinarian-diagnosed food adverse reactions are on the increase. The characteristics of the disease in humans vs dogs, cats, and horses are most often caused by similar, but sometimes species-dependent different pathophysiological mechanisms, prompting the specific clinical symptoms, diagnoses, and treatments. Furthermore, little is known about the allergen molecules causative for type I food allergy in animals, which, like in human patients, could represent predictive biomarkers for risk evaluation. The definite diagnosis of food allergy relies-as in humans-on elimination diet and provocation tests. Besides allergen avoidance in daily practice, novel treatment options and tolerization strategies are underway. Taken together, numerous knowledge gaps were identified in veterinary food allergy, which need to be filled by systematic comparative studies.

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“…Metode ELISA yang digunakan adalah indirect ELISA (Rupa et al, 2008). Sebanyak 100 µL/sumur isolat protein sampel (100 µg/mL) yang terlarut dalam bufer karbonat (0,05 M, pH 9,8) dilapiskan ke dalam lempeng mikrotiter (Nunc Maxisorb).…”

Section: Pengujian Alergenisitas Metode Enzyme Linked Immunosorbent Aunclassified

Perubahan Alergenisitas Protein Kacang Kedelai Dan Kacang Bogor Akibat Pengolahan Dengan Panas

Palupi

Sitorus²,

Kusnandar

2015

jtip

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Legumes contain protein as a potential allergen. Heating process was expected to eliminate the protein allergen. The aim of this study was to assess the changes in molecular weight and allergenicty of soybean grobogan variety and bambara groundnut proteins due to heat processing, i.e. boiling, steaming, oven, and roasting protein isolate was prepared by pH adjusting. SDS-PAGE method was used to determine the profile of protein molecular weight and the alergenicity was determined by ELISA method. Protein molecular weight profile of grobogan soybean and bambara groundnut that have been boiled, steamed, ovened, and roasted for 30 minutes showed variations when compared to the unheated soybean and bambara groundnut protein isolate. The amount of protein detected was reduced compared with unheated soybean and bambara groundnut. The protein allergens in grobogan soybean had molecular weight 110.0, 98.3, 84.5, 67.4, and 60.2. The heat treatment for 30 minutes removed allergenicity as indicated by no detectable protein band in immunoblotting results and the smaller Optical Density value compared with unheated soybean. Thus, the allergenicity of soybean protein due to heat processing was minimized. Bambara groundnut had protein allergens with molecular weight 113.1, 59.8, and 25.2 kDa. Protein allergen with molecular weight 25.2 and 59.8 kDa were detected in bambara groundnut processed through boiling and steaming for 30 minutes, respectively, but ELISA result showed there were still protein allergen of bambara groundnut after the heat treatment for 30 minutes.

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Porcine IgE in the context of experimental food allergy: Purification and isotype-specific antibodies

Cited by 19 publications

References 26 publications

Attenuation of Allergic Immune Response Phenotype by Mannosylated Egg White in Orally Induced Allergy in Balb/c Mice

Attenuation of Allergic Immune Response Phenotype by Mannosylated Egg White in Orally Induced Allergy in Balb/c Mice

Comparing immediate‐type food allergy in humans and companion animals—revealing unmet needs

Perubahan Alergenisitas Protein Kacang Kedelai Dan Kacang Bogor Akibat Pengolahan Dengan Panas

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