Flexible IgE epitope containing domains of Phl p 5 cause high allergenic activity

By Christoph Göbl, Margarete Focke-Tejkl, Nazanin Najafi, Evelyne Schrank, Tobias Madl, Simone Kosol, Christoph Madritsch, Yulia Dorofeeva, Sabine Flicker, Josef Thalhamer, Rudolf Valenta, Klaus Zangger, Nico Tjandra

July 28, 2017

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Title

Flexible IgE epitope containing domains of Phl p 5 cause high allergenic activity

Author

Christoph Göbl, Margarete Focke-Tejkl, Nazanin Najafi, Evelyne Schrank, Tobias Madl, Simone Kosol, Christoph Madritsch, Yulia Dorofeeva, Sabine Flicker, Josef Thalhamer, Rudolf Valenta, Klaus Zangger, Nico Tjandra

Year

2017

Journal

Journal of Allergy and Clinical Immunology

Abstract

This is the first study determining the three-dimensional structure of Phl p 5a which reveals a novel mechanism for high allergenic activity based on flexibly connected IgE-reactive domains which cross-link effector cell-bound IgE more efficiently than isolated rigid globular proteins. These findings may also form a basis for specific immunotherapy strategies.

Full Article

http://www.sciencedirect.com/science/article/pii/S0091674917307959

Instrument

J-810

Keywords

Circular dichroism, Secondary structure, Biochemistry