biostudies-literaturePac-Sosinska MNational Science Centre (Poland)754https://www.ebi.ac.uk/biostudies/studies/S-EPMC12363095biostudies-literatureUnknown26(1)<h4>Background</h4>Phytopathogenic microfungi Erysiphe palczewskii and Erysiphe convolvuli, are ectoparasites causing powdery mildew in common plants. Fungi often produce immunogenic factors triggering allergic reactions, with airborne protein allergens playing a pivotal role in respiratory allergies. This study delves into the biochemical characterization of E. palczewskii and E. convolvuli, focusing on their potential allergenic properties.<h4>Methods</h4>The composition of the tested fungi's fatty acids and sugars was analyzed using liquid chromatography coupled with mass spectrometry (LC/MS). Protein extracts were also subjected to liquid chromatography-mass spectrometry analysis (LC/MS).<h4>Results</h4>The proteomic analysis of E. palczewskii identified 1118 peptides, with 68.8% uniquBMC genomicsBiochemical characteristics of extracts from proallergenic microfungi Erysiphe Palczewskii and Erysiphe convolvuli.PMC12363095OPUS N 2019/35/B/NZ6/00472Pac-Sosinska MWdowiak-Wrobel SMalinowska ASwiderska USztandera-Tymoczek MPalusinska-Szysz MSwiderska BSzuster-Ciesielska AfalseBiochemical characteristics of extracts from proallergenic microfungi Erysiphe Palczewskii and Erysiphe convolvuli.<h4>Background</h4>Phytopathogenic microfungi Erysiphe palczewskii and Erysiphe convolvuli, are ectoparasites causing powdery mildew in common plants. Fungi often produce immunogenic factors triggering allergic reactions, with airborne protein allergens playing a pivotal role in respiratory allergies. This study delves into the biochemical characterization of E. palczewskii and E. convolvuli, focusing on their potential allergenic properties.<h4>Methods</h4>The composition of the tested fungi's fatty acids and sugars was analyzed using liquid chromatography coupled with mass spectrometry (LC/MS). Protein extracts were also subjected to liquid chromatography-mass spectrometry analysis (LC/MS).<h4>Results</h4>The proteomic analysis of E. palczewskii identified 1118 peptides, with 68.8% uniqu2025-01-01T00:00:00Z2025 Aug2026-05-29T14:44:49.525Z2026-04-08T05:10:37.616ZS-EPMC123630954082644210.1186/s12864-025-11862-w