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Published on: June 14, 2020
Biochemical characteristics of extracts from proallergenic microfungi Erysiphe Palczewskii and Erysiphe convolvuli
Małgorzata Pac-Sosińska1, Marta Palusińska-Szysz2, Monika Sztandera-Tymoczek1
1Department of Virology and Immunology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, Lublin, 20-033, Poland.
Background:
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.
Methods:
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).
Results:
The proteomic analysis of E. palczewskii identified 1118 peptides, with 68.8% unique to this species. The abundant proteins included ribosomal proteins, heat shock proteins, enolase, fumarate reductase, and nucleoside diphosphate kinase. The E. convolvuli analysis revealed 770 peptides, with 47% unique sequences. The abundant proteins included ribosomal proteins, heat shock proteins, NDPK, glycerol dehydrogenase, malate dehydrogenase, and a Rho GDP dissociation inhibitor. The analysis of the fatty acid composition revealed that both species exhibited a diverse profile and synthesized fatty acid 18:2, which constituted approximately 30% of the total fatty acids in E. palczewskii. The analyzed fungi primarily produced hexoses, pentoses, and hexosamines.
Conclusion:
The comparative proteomic analysis provided insights into the unique and shared proteins of E. palczewskii and E. convolvuli. Several proteins, including heat shock proteins and enzymes involved in metabolic processes, exhibited allergenic potential. The studied fungi contained a high concentration of fatty acid 18:2, a precursor of arachidonic acid, which is involved in developing inflammatory responses.
Insights
This study characterized powdery mildew fungi Erysiphe palczewskii and Erysiphe convolvuli, identifying allergenic proteins and high levels of fatty acid 18:2, a precursor to inflammatory compounds.
Area of Science:
- Mycology
- Biochemistry
- Allergology
Background:
- Powdery mildew, caused by Erysiphe palczewskii and Erysiphe convolvuli, affects common plants.
- Fungal allergens, particularly airborne proteins, are significant triggers for respiratory allergies.
- This research investigates the biochemical makeup of these fungi for potential allergenic properties.
Purpose of the Study:
- To perform a comparative proteomic analysis of E. palczewskii and E. convolvuli.
- To identify unique and shared proteins between the two fungal species.
- To assess the allergenic potential of identified proteins and biochemical components.
Main Methods:
- Proteomic analysis using liquid chromatography-mass spectrometry (LC/MS) for protein identification.
- Fatty acid and sugar composition analysis via LC/MS.
- Comparative analysis of protein and biochemical profiles.
Main Results:
- E. palczewskii proteome: 1118 peptides (68.8% unique), abundant in ribosomal proteins, heat shock proteins, and metabolic enzymes.
- E. convolvuli proteome: 770 peptides (47% unique), abundant in ribosomal proteins, heat shock proteins, and dehydrogenases.
- Both species contain diverse fatty acids, with fatty acid 18:2 comprising ~30% in E. palczewskii; hexoses, pentoses, and hexosamines are primary sugars.
Conclusions:
- Comparative proteomics revealed distinct and common proteins in E. palczewskii and E. convolvuli.
- Heat shock proteins and metabolic enzymes show potential as allergens.
- High concentrations of fatty acid 18:2, a precursor to inflammatory arachidonic acid, were found.
