Fusion proteins consisting of Bet v 1 and Phl p 5 form IgE-reactive aggregates with reduced allergenic activity
Najafi N., Hofer G., Gattinger P., Smiljkovic D., Blatt K., Selb R., Stoecklinger A., Keller W., Valent P., Niederberger V., Thalhamer J., Valenta R., Flicker S.
Scientific Reports
Vol.9, Issue1, Num.4006
Опубликовано: 2019
Тип ресурса: Статья
DOI:10.1038/s41598-019-39798-8
Аннотация:
The cross-linking of effector cell-bound IgE antibodies by allergens induces the release of inflammatory mediators which are responsible for the symptoms of allergy. We demonstrate that a recombinant hybrid molecule consisting of the major birch (Bet v 1) and grass (Phl p 5) pollen allergen exhibited reduced allergenic activity as compared to equimolar mixes of the isolated allergens in basophil activation experiments. The reduced allergenic activity of the hybrid was not due to reduced IgE reactivity as demonstrated by IgE binding experiments using sera from allergic patients. Physicochemical characterization of the hybrid by size exclusion chromatography, dynamic light scattering, negative-stain electron microscopy and circular dichroism showed that the hybrid occurred as folded aggregate whereas the isolated allergens were folded monomeric proteins. IgG antibodies raised in rabbits against epitopes of Bet v 1 and Phl p 5 showed reduced reactivity with the hybrid compared to the mono
Язык текста: Английский
ISSN: 2045-2322
Najafi N.
Hofer G.
Gattinger P.
Smiljkovic D.
Blatt K.
Selb R.
Stoecklinger A.
Keller W.
Valent P.
Niederberger V.
Thalhamer J.
Valenta R. Rudol`f 1963-
Flicker S.
Найафи Н.
Хофер Г.
Гаттингер П.
Смилйковиc Д.
Блатт К.
Селб Р.
Стоеcклингер А.
Келлер W.
Валент П.
Ниедербергер В.
Тхалхамер Й.
Валента Р. Рудольф 1963-
Флиcкер С.
Fusion proteins consisting of Bet v 1 and Phl p 5 form IgE-reactive aggregates with reduced allergenic activity
Текст визуальный непосредственный
Scientific Reports
Vol.9, Issue1 Num.4006
2019
Статья
The cross-linking of effector cell-bound IgE antibodies by allergens induces the release of inflammatory mediators which are responsible for the symptoms of allergy. We demonstrate that a recombinant hybrid molecule consisting of the major birch (Bet v 1) and grass (Phl p 5) pollen allergen exhibited reduced allergenic activity as compared to equimolar mixes of the isolated allergens in basophil activation experiments. The reduced allergenic activity of the hybrid was not due to reduced IgE reactivity as demonstrated by IgE binding experiments using sera from allergic patients. Physicochemical characterization of the hybrid by size exclusion chromatography, dynamic light scattering, negative-stain electron microscopy and circular dichroism showed that the hybrid occurred as folded aggregate whereas the isolated allergens were folded monomeric proteins. IgG antibodies raised in rabbits against epitopes of Bet v 1 and Phl p 5 showed reduced reactivity with the hybrid compared to the mono