Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study

Agriculture and Food Sciences Adult Hypersensitivity, Immediate Male Proteomics AMBROSIA-ARTEMISIIFOLIA THUNDERSTORM ASTHMA Adolescent PROTEINS ART V 1 label-free quantification Young Adult 03 medical and health sciences Medicine and Health Sciences Humans pollen allergomes Ambrosia artemisiifolia Plant Proteins GRASS-POLLEN RELEASE 0303 health sciences Plant Extracts Rhinitis, Allergic, Seasonal NADH Dehydrogenase Allergens Antigens, Plant Middle Aged SENSITIZATION subpollen particles new short ragweed allergens CROSS-REACTIVITY Female Ambrosia AMB-A-I MUGWORT POLLEN
DOI: 10.1111/cea.12874 Publication Date: 2016-12-21T13:32:34Z
ABSTRACT
SummaryBackgroundShort 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.MethodsQuantitative 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.ResultsThe 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 RelevanceWe 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.
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