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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)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Clinical and Experimental Allergy
volume
44
issue
11
pages
1409 - 1419
publisher
Wiley-Blackwell
external identifiers
  • wos:000344371300012
  • pmid:25262820
  • scopus:84939148042
ISSN
1365-2222
DOI
10.1111/cea.12423
language
English
LU publication?
yes
id
e15513c2-2b51-4f23-ad60-061fede8acf5 (old id 4690817)
date added to LUP
2014-10-10 10:20:24
date last changed
2017-11-19 03:03:31
@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 &amp; 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-Blackwell},
  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},
  volume       = {44},
  year         = {2014},
}