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

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

doi:10.1016/j.jaci.2017.05.005

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

J Allergy Clin Immunol. 2017 Oct;140(4):1187-1191. doi: 10.1016/j.jaci.2017.05.005. Epub 2017 May 19.

Authors

Affiliations

¹ Institute of Chemistry/Organic and Bioorganic Chemistry, University of Graz, Graz, Austria; Institute of Structural Biology, Helmholtz Zentrum München, Neuherberg, Germany; Biomolecular NMR, Department of Chemistry, Technische Universität München, Garching, Germany; Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Md.
² Division of Immunopathology, Department of Pathophysiology and Allergy Research, Medical University of Vienna, Vienna, Austria.
³ Institute of Chemistry/Organic and Bioorganic Chemistry, University of Graz, Graz, Austria.
⁴ Institute of Structural Biology, Helmholtz Zentrum München, Neuherberg, Germany; Biomolecular NMR, Department of Chemistry, Technische Universität München, Garching, Germany; Institute of Molecular Biology & Biochemistry, Center of Molecular Medicine, Medical University of Graz, Graz, Austria.
⁵ Department of Molecular Biology, Division of Allergy and Immunology, University of Salzburg, Salzburg, Austria.
⁶ Division of Immunopathology, Department of Pathophysiology and Allergy Research, Medical University of Vienna, Vienna, Austria. Electronic address: rudolf.valenta@meduniwien.ac.at.
⁷ Institute of Chemistry/Organic and Bioorganic Chemistry, University of Graz, Graz, Austria. Electronic address: klaus.zangger@uni-graz.at.
⁸ Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Md. Electronic address: tjandran@nhlbi.nih.gov.

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.

Publication types

Letter
Research Support, N.I.H., Intramural
Research Support, Non-U.S. Gov't

MeSH terms

Allergens / immunology*
Epitopes / immunology*
Immunoglobulin E / immunology*
Plant Proteins / immunology*

Substances

Allergens
Epitopes
Phl p V protein, Phleum pratense
Plant Proteins
Immunoglobulin E

Grants and funding

Z99 HL999999/Intramural NIH HHS/United States