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dc.creatorSmiljanić, Katarina
dc.creatorApostolović, Danijela
dc.creatorTrifunović, S.
dc.creatorOgnjenović, Jana
dc.creatorPerusko, M.
dc.creatorMihajlović, Luka
dc.creatorBurazer, Lidija
dc.creatorvan Hage, Marianne
dc.creatorĆirković-Veličković, Tanja
dc.date.accessioned2021-08-30T08:36:39Z
dc.date.available2017-12-21
dc.date.issued2017
dc.identifier.issn0954-7894
dc.identifier.urihttp://intor.torlakinstitut.com/handle/123456789/610
dc.description.abstractBackground: Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods: Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results: The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance: We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.en
dc.publisherBlackwell Publishing Ltd
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/256716/EU//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS//
dc.relation.isversionofhttps://doi.org/10.1111/cea.12874
dc.relation.isversionofhttp://intor.torlakinstitut.com/handle/123456789/479
dc.rightsembargoedAccess
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceClinical and Experimental Allergy
dc.subjectAmbrosia artemisiifoliaen
dc.subjectlabel-free quantificationen
dc.subjectnew short ragweed allergensen
dc.subjectpollen allergomesen
dc.subjectsubpollen particlesen
dc.titleSubpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic studyen
dc.typearticle
dc.rights.licenseBY
dc.citation.epage828
dc.citation.issue6
dc.citation.other47(6): 815-828
dc.citation.rankM21
dc.citation.spage815
dc.citation.volume47
dc.description.otherThis is the peer‐reviewed version of the article: Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; Hage, M. van; Velickovic, T. C. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical & Experimental Allergy 2017, 47 (6), 815–828.[https://doi.org/10.1111/cea.12874]
dc.identifier.doi10.1111/cea.12874
dc.identifier.fulltexthttp://intor.torlakinstitut.com/bitstream/id/1253/postprint-smiljanic2016 (1) vezba.pdf
dc.identifier.pmid28000951
dc.identifier.scopus2-s2.0-85009944152
dc.identifier.wos000402653100011
dc.type.versionacceptedVersion


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