Multiple independent IgE epitopes on the highly allergenic grass pollen allergen Phl p 5.
Levin, Mattias LU ; Rotthus, Stefanie LU ; Wendel, Sofie LU ; Najafi, Nazanin ; Källström, Eva ; Focke-Tejkl, Margarete ; Valenta, Rudolf ; Flicker, Sabine and Ohlin, Mats LU
(2014)
In Clinical and Experimental Allergy
44(11).
p.1409-1419
- Abstract
- Background
Group 5 allergens are small proteins that consist of two domains. They belong to the most potent respiratory allergens.
Objective
To determine the binding sites and to study allergic patients' IgE recognition of the group 5 allergen (Phl p 5) from timothy grass pollen using human monoclonal IgE antibodies that have been isolated from grass pollen allergic patients.
Methods
Using recombinant isoallergens, fragments, mutants and synthetic peptides of Phl p 5, as well as peptide-specific antibodies, the interaction of recombinant human monoclonal IgE and Phl p 5 was studied using direct binding and blocking assays. Cross-reactivity of monoclonal IgE with group 5... (More) - Background
Group 5 allergens are small proteins that consist of two domains. They belong to the most potent respiratory allergens.
Objective
To determine the binding sites and to study allergic patients' IgE recognition of the group 5 allergen (Phl p 5) from timothy grass pollen using human monoclonal IgE antibodies that have been isolated from grass pollen allergic patients.
Methods
Using recombinant isoallergens, fragments, mutants and synthetic peptides of Phl p 5, as well as peptide-specific antibodies, the interaction of recombinant human monoclonal IgE and Phl p 5 was studied using direct binding and blocking assays. Cross-reactivity of monoclonal IgE with group 5 allergens in several grasses was studied and inhibition experiments with patients' polyclonal IgE were performed.
Results
Monoclonal human IgE showed extensive cross-reactivity with group 5 allergens in several grasses. Despite its small size of 29 kDa, four independent epitope clusters on isoallergen Phl p 5.0101, two in each domain, were recognized by human IgE. Isoallergen Phl p 5.0201 carried two of these epitopes. Inhibition studies with allergic patients' polyclonal IgE suggest the presence of additional IgE epitopes on Phl p 5.
Conclusions & Clinical Relevance
Our results reveal the presence of a large number of independent IgE epitopes on the Phl p 5 allergen explaining the high allergenic activity of this protein and its ability to induce severe allergic symptoms. High-density IgE recognition may be a general feature of many potent allergens and form a basis for the development of improved diagnostic and therapeutic procedures in allergic disease. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4690817
- author
- Levin, Mattias
LU
; Rotthus, Stefanie
LU
; Wendel, Sofie
LU
; Najafi, Nazanin
; Källström, Eva
; Focke-Tejkl, Margarete
; Valenta, Rudolf
; Flicker, Sabine
and Ohlin, Mats
LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Clinical and Experimental Allergy
- volume
- 44
- issue
- 11
- pages
- 1409 - 1419
- publisher
- Wiley
- external identifiers
-
- wos:000344371300012
- pmid:25262820
- scopus:84939148042
- pmid:25262820
- ISSN
- 1365-2222
- DOI
- 10.1111/cea.12423
- project
- Human IgE repertoires and an anti-allergome resource
- language
- English
- LU publication?
- yes
- id
- e15513c2-2b51-4f23-ad60-061fede8acf5 (old id 4690817)
- date added to LUP
- 2016-04-01 09:59:48
- date last changed
- 2022-02-24 21:20:23
@article{e15513c2-2b51-4f23-ad60-061fede8acf5,
abstract = {{Background<br/><br>
Group 5 allergens are small proteins that consist of two domains. They belong to the most potent respiratory allergens.<br/><br>
<br/><br>
Objective<br/><br>
To determine the binding sites and to study allergic patients' IgE recognition of the group 5 allergen (Phl p 5) from timothy grass pollen using human monoclonal IgE antibodies that have been isolated from grass pollen allergic patients.<br/><br>
<br/><br>
Methods<br/><br>
Using recombinant isoallergens, fragments, mutants and synthetic peptides of Phl p 5, as well as peptide-specific antibodies, the interaction of recombinant human monoclonal IgE and Phl p 5 was studied using direct binding and blocking assays. Cross-reactivity of monoclonal IgE with group 5 allergens in several grasses was studied and inhibition experiments with patients' polyclonal IgE were performed.<br/><br>
<br/><br>
Results<br/><br>
Monoclonal human IgE showed extensive cross-reactivity with group 5 allergens in several grasses. Despite its small size of 29 kDa, four independent epitope clusters on isoallergen Phl p 5.0101, two in each domain, were recognized by human IgE. Isoallergen Phl p 5.0201 carried two of these epitopes. Inhibition studies with allergic patients' polyclonal IgE suggest the presence of additional IgE epitopes on Phl p 5.<br/><br>
<br/><br>
Conclusions & Clinical Relevance<br/><br>
Our results reveal the presence of a large number of independent IgE epitopes on the Phl p 5 allergen explaining the high allergenic activity of this protein and its ability to induce severe allergic symptoms. High-density IgE recognition may be a general feature of many potent allergens and form a basis for the development of improved diagnostic and therapeutic procedures in allergic disease.}},
author = {{Levin, Mattias and Rotthus, Stefanie and Wendel, Sofie and Najafi, Nazanin and Källström, Eva and Focke-Tejkl, Margarete and Valenta, Rudolf and Flicker, Sabine and Ohlin, Mats}},
issn = {{1365-2222}},
language = {{eng}},
number = {{11}},
pages = {{1409--1419}},
publisher = {{Wiley}},
series = {{Clinical and Experimental Allergy}},
title = {{Multiple independent IgE epitopes on the highly allergenic grass pollen allergen Phl p 5.}},
url = {{http://dx.doi.org/10.1111/cea.12423}},
doi = {{10.1111/cea.12423}},
volume = {{44}},
year = {{2014}},
}