Thioredoxin from the Indianmeal moth Plodia interpunctella: cloning and test of the allergenic potential in mice.

<h4>Background/objective</h4>The Indianmeal moth Plodia interpunctella is a highly prevalent food pest in human dwellings, and has been shown to contain a number of allergens. So far, only one of these, the arginine kinase (Plo i 1) has been identified.<h4>Objective</h4>The a...

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Autores principales: Elisabeth Hoflehner, Marina Binder, Wolfgang Hemmer, Vera Mahler, Raphael C Panzani, Reinhart Jarisch, Ursula Wiedermann, Michael Duchêne
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Publicado: Public Library of Science (PLoS) 2012
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spelling oai:doaj.org-article:c79f9971a623402888c55e090e1c48642021-11-18T07:10:54ZThioredoxin from the Indianmeal moth Plodia interpunctella: cloning and test of the allergenic potential in mice.1932-620310.1371/journal.pone.0042026https://doaj.org/article/c79f9971a623402888c55e090e1c48642012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22844539/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background/objective</h4>The Indianmeal moth Plodia interpunctella is a highly prevalent food pest in human dwellings, and has been shown to contain a number of allergens. So far, only one of these, the arginine kinase (Plo i 1) has been identified.<h4>Objective</h4>The aim of this study was to identify further allergens and characterise these in comparison to Plo i 1.<h4>Method</h4>A cDNA library from whole adult P. interpunctella was screened with the serum of a patient with indoor allergy and IgE to moths, and thioredoxin was identified as an IgE-binding protein. Recombinant thioredoxin was generated in E. coli, and tested together with Plo i 1 and whole moth extracts in IgE immunoblots against a large panel of indoor allergic patients' sera. BALB/c mice were immunised with recombinant thioredoxin and Plo i 1, and antibody production, mediator release from RBL cells, T-cell proliferation and cytokine production were measured.<h4>Result</h4>For the first time a thioredoxin from an animal species was identified as allergen. About 8% of the sera from patients with IgE against moth extracts reacted with recombinant P. interpunctella thioredoxin, compared to 25% reacting with recombinant Plo i 1. In immunised BALB/c mice, the recombinant allergens both induced classical Th2-biased immune responses such as induction IgE and IgG1 antibodies, upregulation of IL-5 and IL-4 and basophil degranulation.<h4>Conclusion</h4>Thioredoxin from moths like Plo i 1 acts like a classical Type I allergen as do the thioredoxins from wheat or corn. This clearly supports the pan-allergen nature of thioredoxin. The designation Plo i 2 is suggested for the new P. interpunctella allergen.Elisabeth HoflehnerMarina BinderWolfgang HemmerVera MahlerRaphael C PanzaniReinhart JarischUrsula WiedermannMichael DuchênePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 7, p e42026 (2012)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Elisabeth Hoflehner
Marina Binder
Wolfgang Hemmer
Vera Mahler
Raphael C Panzani
Reinhart Jarisch
Ursula Wiedermann
Michael Duchêne
Thioredoxin from the Indianmeal moth Plodia interpunctella: cloning and test of the allergenic potential in mice.
description <h4>Background/objective</h4>The Indianmeal moth Plodia interpunctella is a highly prevalent food pest in human dwellings, and has been shown to contain a number of allergens. So far, only one of these, the arginine kinase (Plo i 1) has been identified.<h4>Objective</h4>The aim of this study was to identify further allergens and characterise these in comparison to Plo i 1.<h4>Method</h4>A cDNA library from whole adult P. interpunctella was screened with the serum of a patient with indoor allergy and IgE to moths, and thioredoxin was identified as an IgE-binding protein. Recombinant thioredoxin was generated in E. coli, and tested together with Plo i 1 and whole moth extracts in IgE immunoblots against a large panel of indoor allergic patients' sera. BALB/c mice were immunised with recombinant thioredoxin and Plo i 1, and antibody production, mediator release from RBL cells, T-cell proliferation and cytokine production were measured.<h4>Result</h4>For the first time a thioredoxin from an animal species was identified as allergen. About 8% of the sera from patients with IgE against moth extracts reacted with recombinant P. interpunctella thioredoxin, compared to 25% reacting with recombinant Plo i 1. In immunised BALB/c mice, the recombinant allergens both induced classical Th2-biased immune responses such as induction IgE and IgG1 antibodies, upregulation of IL-5 and IL-4 and basophil degranulation.<h4>Conclusion</h4>Thioredoxin from moths like Plo i 1 acts like a classical Type I allergen as do the thioredoxins from wheat or corn. This clearly supports the pan-allergen nature of thioredoxin. The designation Plo i 2 is suggested for the new P. interpunctella allergen.
format article
author Elisabeth Hoflehner
Marina Binder
Wolfgang Hemmer
Vera Mahler
Raphael C Panzani
Reinhart Jarisch
Ursula Wiedermann
Michael Duchêne
author_facet Elisabeth Hoflehner
Marina Binder
Wolfgang Hemmer
Vera Mahler
Raphael C Panzani
Reinhart Jarisch
Ursula Wiedermann
Michael Duchêne
author_sort Elisabeth Hoflehner
title Thioredoxin from the Indianmeal moth Plodia interpunctella: cloning and test of the allergenic potential in mice.
title_short Thioredoxin from the Indianmeal moth Plodia interpunctella: cloning and test of the allergenic potential in mice.
title_full Thioredoxin from the Indianmeal moth Plodia interpunctella: cloning and test of the allergenic potential in mice.
title_fullStr Thioredoxin from the Indianmeal moth Plodia interpunctella: cloning and test of the allergenic potential in mice.
title_full_unstemmed Thioredoxin from the Indianmeal moth Plodia interpunctella: cloning and test of the allergenic potential in mice.
title_sort thioredoxin from the indianmeal moth plodia interpunctella: cloning and test of the allergenic potential in mice.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/c79f9971a623402888c55e090e1c4864
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