Covalent polyphenol modification of a reactive cysteine in the major apple allergen Mal d 1

Unterhauser, Jana; Ahammer, Linda; Rainer, Tobias; Eidelpes, Reiner; Führer, Sebastian; Nothegger, Bettina; Covaciu, Claudia E.; Cova, V.; Kamenik, Anna S.; Liedl, Klaus R.; Müller, Thomas; Breuker, Kathrin; Eisendle, Klaus; Reider, Norbert; Letschka, Thomas; Tollinger, Martin

doi:10.1016/j.foodchem.2022.135374

Cited by 14 publications

(16 citation statements)

References 38 publications

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“…Paramagnetic relaxation data were obtained using samples of 151 μM Pru p 1 in the presence of 1.4‐fold excess of 3′‐TEMPO labeled RNA 1 , and 200 μM Pru p 1 with 1.6‐fold excess of 5′‐TEMPO labeled RNA 1 . Backbone amide 1 H‐ 15 N HSQC spectra were recorded before and after reducing the paramagnetic tag with 11 mole equivalents of ascorbic acid, and peak volumes were used to analyzed the paramagnetic data [28] …”

Section: Methodsmentioning

confidence: 99%

“…Backbone amide 1 H-15 N HSQC spectra were recorded before and after reducing the paramagnetic tag with 11 mole equivalents of ascorbic acid, and peak volumes were used to analyzed the paramagnetic data. [28] UV Melting Curves RNA samples were lyophilized as sodium salts, dissolved in 800 μL buffer (10 mM Na 2 HPO 4 , pH 7.0, 150 mM NaCl) and transferred into UV permeable high precision cells made of quartz SUPRASIL® with a light path of 10 mm or 1 mm. UV melting profiles were recorded at 250 nm and 260 nm on an Agilent Cary 3500 UV-Vis spectrophotometer equipped with multiple cell holders and Peltier temperature control devices.…”

Section: Kinetic Analysismentioning

confidence: 99%

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The PR‐10 Protein Pru p 1 is an Endonuclease that Preferentially Cleaves Single–Stranded RNA

Röck,

Heel,

Juen

et al. 2024

ChemBioChem

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Pathogenesis‐related class 10 (PR‐10) proteins play a crucial role in plant defense by acting as ribonucleases. The specific mechanism of action and substrate specificity of these proteins have remained largely unexplored so far. In this study, we elucidate the enzymatic activity of Pru p 1, a PR‐10 protein from peach. We demonstrate that this protein catalyzes the endonucleolytic backbone cleavage of RNA substrates into short oligonucleotides. Initial cleavage products, identified through kinetic analysis, can bind again, priming them for further degradation. NMR binding site mapping reveals that the large internal cavity of Pru p 1, which is characteristic for PR‐10 proteins, serves as an anchoring site for single‐stranded ribonucleotide chains. We propose a structure‐based mechanistic model that accounts for the observed cleavage patterns and the inhibitory effect of zeatin, a nucleoside analog, on the ribonuclease activity of Pru p 1.

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Section: Methodsmentioning

confidence: 99%

Section: Kinetic Analysismentioning

confidence: 99%

The PR‐10 Protein Pru p 1 is an Endonuclease that Preferentially Cleaves Single–Stranded RNA

Röck,

Heel,

Juen

et al. 2024

ChemBioChem

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“…In the study of betv 4 and Phlp4, birch and grass pollen allergens, researchers found that the physiological oxidant peroxynitrite forms protein dimers and higher oligomers through protein nitration, thereby enhancing the activation of toll‐like receptor 4, resulting in increased sensitivity to grass pollen allergen (Reinmuth‐Selzle et al ., 2023). Other studies have shown that plasma could cause oxidation of sesame protein, thereby reducing the binding ability of sesame protein to IgE antibodies (Unterhauser et al ., 2023). Li et al .…”

Section: Effects Of Oxidation On the Physicochemical Properties And Q...mentioning

confidence: 99%

Protein oxidation‐induced changes in the physicochemical properties and quality of plant food

Wu,

Ji,

Xue

et al. 2024

Int J of Food Sci Tech

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SummaryProtein oxidation is widely present in food systems and is susceptible to internal factors involving lipids and enzymes as well as external factors such as temperature and oxygen promoters. Protein oxidation leads to modification of the peptide skeletons and amino acid side chains, which in turn alters the structural characteristics of proteins, including protein cleavage, aggregation and derivative formation, and severely affects their physicochemical properties and bioavailability, thereby reducing the edible and storage qualities of foods. This review summarises the main factors that cause and regulate oxidation of plant protein, the effects of protein oxidation on food quality and strategies to ameliorate protein over‐oxidation, aiming to provide meaningful information for the development of high‐quality plant protein products.

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“…Interestingly, the immunotoxicity for both 5-CQA and 3,5-DCQA was also predicted to be positive ( p = 0.99) using the in silico tool from Banerjee et al [ 194 ]. In apples, Unterhauser et al recently demonstrated that the interaction of CQA with proteins (formation of adducts as a hapten–protein conjugate) via reactive o -benzoquinone in vitro causes a loss of conformational epitopes and a decrease in the IgE-binding capacity by the direct reaction of CQA with the cysteine moiety of IgE [ 232 ]. Interestingly, the high content of CQA in apples results in a lower allergenic potential.…”

Section: Toxicological Informationmentioning

confidence: 99%

Risk Assessment of Chlorogenic and Isochlorogenic Acids in Coffee By-Products

Behne,

Franke,

Schwarz

et al. 2023

Molecules

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Chlorogenic and isochlorogenic acids are naturally occurring antioxidant dietary polyphenolic compounds found in high concentrations in plants, fruits, vegetables, coffee, and coffee by-products. The objective of this review was to assess the potential health risks associated with the oral consumption of coffee by-products containing chlorogenic and isochlorogenic acids, considering both acute and chronic exposure. An electronic literature search was conducted, revealing that 5-caffeoylquinic acid (5-CQA) and 3,5-dicaffeoylquinic acid (3,5-DCQA) are the major chlorogenic acids found in coffee by-products. Toxicological, pharmacokinetic, and clinical data from animal and human studies were available for the assessment, which indicated no significant evidence of toxic or adverse effects following acute oral exposure. The current state of knowledge suggests that long-term exposure to chlorogenic and isochlorogenic acids by daily consumption does not appear to pose a risk to human health when observed at doses within the normal range of dietary exposure. As a result, the intake of CQAs from coffee by-products can be considered reasonably safe.

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Covalent polyphenol modification of a reactive cysteine in the major apple allergen Mal d 1

Cited by 14 publications

References 38 publications

The PR‐10 Protein Pru p 1 is an Endonuclease that Preferentially Cleaves Single–Stranded RNA

The PR‐10 Protein Pru p 1 is an Endonuclease that Preferentially Cleaves Single–Stranded RNA

Protein oxidation‐induced changes in the physicochemical properties and quality of plant food

Risk Assessment of Chlorogenic and Isochlorogenic Acids in Coffee By-Products

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