2006
DOI: 10.1016/j.bbrc.2006.01.174
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Engineered recombinant ovomucoid third domain can modulate allergenic response in Balb/c mice model

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Cited by 15 publications
(8 citation statements)
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“…The mouse model has been and will continue to be an extremely useful tool for life sciences research. The fine mapping of OVM B-cell epitopes was recently reported in the inbred BALB/c mouse strain, a commonly accepted murine model of food allergy , . In line with the epitope results obtained from egg-allergic patients’ sera, the study showed that OVM domain III exhibited the highest IgE-binding intensity in BALB/c mice.…”
Section: Molecular Properties Of Egg Allergenssupporting
confidence: 68%
See 1 more Smart Citation
“…The mouse model has been and will continue to be an extremely useful tool for life sciences research. The fine mapping of OVM B-cell epitopes was recently reported in the inbred BALB/c mouse strain, a commonly accepted murine model of food allergy , . In line with the epitope results obtained from egg-allergic patients’ sera, the study showed that OVM domain III exhibited the highest IgE-binding intensity in BALB/c mice.…”
Section: Molecular Properties Of Egg Allergenssupporting
confidence: 68%
“…The molecule consists of three structurally independent tandem homologous domains (domains Gal d 1.1, 1.2 and 1.3), possesses nine intramolecular disulfide bridges, and 20−25% of carbohydrates entities . Domain Gal d 1.3 was reported as the immunodominant fraction , .…”
Section: Molecular Properties Of Egg Allergensmentioning
confidence: 99%
“…Modified, hypoallergenic allergens that have been synthesized include peanut (Ara h 1,2,3) [159], milk (casein) [160,161], fish (parvalbumin) [162], peach (Pru p 1) [163] and apple (Mal d 1) [164]. Human trials have yet to be performed, but recombinant ovomucoid was found to decrease anaphylaxis scores and histamine responses, while increasing IFN-γ, suggesting a Th1 shift [165,166]. Another modification being assessed is the addition of sugar moieties to the allergen to mimic pathogens and drive the Th1 response.…”
Section: Treatment Of Fa: Current and Future Potentialmentioning
confidence: 99%
“…The molecule is composed of 186 amino acids which are arranged in three domains and secured with disulfide bonds. This structural characteristic may be the cause of its high resistance to heat and proteolytic digestion, as well as its allergenic capacity [3][4][5].…”
Section: Introductionmentioning
confidence: 99%