Proteomic profiling of the weed feverfew, a neglected pollen allergen source

Abstract Feverfew (Parthenium hysterophorus), an invasive weed from the Asteraceae family, has been reported as allergen source. Despite its relevance, knowledge of allergens is restricted to a partial sequence of a hydroxyproline-rich glycoprotein. We aimed to obtain the entire sequence for recombi...

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Autores principales:	Isabel Pablos, Stephanie Eichhorn, Peter Briza, Claudia Asam, Ulrike Gartner, Martin Wolf, Christof Ebner, Barbara Bohle, Naveen Arora, Stefan Vieths, Fatima Ferreira, Gabriele Gadermaier
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/cdf477119cfd4217be68557d3813d227
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spelling	oai:doaj.org-article:cdf477119cfd4217be68557d3813d2272021-12-02T11:52:44ZProteomic profiling of the weed feverfew, a neglected pollen allergen source10.1038/s41598-017-06213-z2045-2322https://doaj.org/article/cdf477119cfd4217be68557d3813d2272017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06213-zhttps://doaj.org/toc/2045-2322Abstract Feverfew (Parthenium hysterophorus), an invasive weed from the Asteraceae family, has been reported as allergen source. Despite its relevance, knowledge of allergens is restricted to a partial sequence of a hydroxyproline-rich glycoprotein. We aimed to obtain the entire sequence for recombinant production and characterize feverfew pollen using proteomics and immunological assays. Par h 1, a defensin-proline fusion allergen was obtained by cDNA cloning and recombinantly produced in E. coli. Using two complementary proteomic strategies, a total of 258 proteins were identified in feverfew pollen among those 47 proteins belonging to allergenic families. Feverfew sensitized patients’ sera from India revealed IgE reactivity with a pectate lyase, PR-1 protein and thioredoxin in immonoblot. In ELISA, recombinant Par h 1 was recognized by 60 and 40% of Austrian and Indian sera, respectively. Inhibition assays demonstrated the presence of IgE cross-reactive Par h 1, pectate lyase, lipid-transfer protein, profilin and polcalcin in feverfew pollen. This study reveals significant data on the allergenic composition of feverfew pollen and makes recombinant Par h 1 available for cross-reactivity studies. Feverfew might become a global player in weed pollen allergy and inclusion of standardized extracts in routine allergy diagnosis is suggested in exposed populations.Isabel PablosStephanie EichhornPeter BrizaClaudia AsamUlrike GartnerMartin WolfChristof EbnerBarbara BohleNaveen AroraStefan ViethsFatima FerreiraGabriele GadermaierNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Isabel Pablos Stephanie Eichhorn Peter Briza Claudia Asam Ulrike Gartner Martin Wolf Christof Ebner Barbara Bohle Naveen Arora Stefan Vieths Fatima Ferreira Gabriele Gadermaier Proteomic profiling of the weed feverfew, a neglected pollen allergen source
description	Abstract Feverfew (Parthenium hysterophorus), an invasive weed from the Asteraceae family, has been reported as allergen source. Despite its relevance, knowledge of allergens is restricted to a partial sequence of a hydroxyproline-rich glycoprotein. We aimed to obtain the entire sequence for recombinant production and characterize feverfew pollen using proteomics and immunological assays. Par h 1, a defensin-proline fusion allergen was obtained by cDNA cloning and recombinantly produced in E. coli. Using two complementary proteomic strategies, a total of 258 proteins were identified in feverfew pollen among those 47 proteins belonging to allergenic families. Feverfew sensitized patients’ sera from India revealed IgE reactivity with a pectate lyase, PR-1 protein and thioredoxin in immonoblot. In ELISA, recombinant Par h 1 was recognized by 60 and 40% of Austrian and Indian sera, respectively. Inhibition assays demonstrated the presence of IgE cross-reactive Par h 1, pectate lyase, lipid-transfer protein, profilin and polcalcin in feverfew pollen. This study reveals significant data on the allergenic composition of feverfew pollen and makes recombinant Par h 1 available for cross-reactivity studies. Feverfew might become a global player in weed pollen allergy and inclusion of standardized extracts in routine allergy diagnosis is suggested in exposed populations.
format	article
author	Isabel Pablos Stephanie Eichhorn Peter Briza Claudia Asam Ulrike Gartner Martin Wolf Christof Ebner Barbara Bohle Naveen Arora Stefan Vieths Fatima Ferreira Gabriele Gadermaier
author_facet	Isabel Pablos Stephanie Eichhorn Peter Briza Claudia Asam Ulrike Gartner Martin Wolf Christof Ebner Barbara Bohle Naveen Arora Stefan Vieths Fatima Ferreira Gabriele Gadermaier
author_sort	Isabel Pablos
title	Proteomic profiling of the weed feverfew, a neglected pollen allergen source
title_short	Proteomic profiling of the weed feverfew, a neglected pollen allergen source
title_full	Proteomic profiling of the weed feverfew, a neglected pollen allergen source
title_fullStr	Proteomic profiling of the weed feverfew, a neglected pollen allergen source
title_full_unstemmed	Proteomic profiling of the weed feverfew, a neglected pollen allergen source
title_sort	proteomic profiling of the weed feverfew, a neglected pollen allergen source
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/cdf477119cfd4217be68557d3813d227
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Proteomic profiling of the weed feverfew, a neglected pollen allergen source

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