Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases

Radosavljević, Jelena; Dobrijevic, Dragana; Jadranin, Milka; Blanusa, Milan; Vukmirica, Jelena; Veličković, Tanja Ćirković

doi:10.1002/jsfa.4005

Cited by 14 publications

(8 citation statements)

References 22 publications

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“…Panel a - Ara h 2.02, peptides a, and b; Panel b - Ara h 2.01, peptides b, c, d, and e; Panel c - Ara h 6, peptides a, and b), which after reduction yields two peptides with molecular weights from 7.2–9.7 kDa for Ara h 2 and 4.8-9.4 kDa for Ara h 6. In the intact DRPs from Ara h 2, a C-terminal proteolytic processing of the Y/RY fragment was observed 29 , but also cleavage at the trypsin cleavage site Arg 149/137 -Asp 150/138 . Additionally, peptides with deleted internal short segments (S 48 TR 50 in Ara h 6 and D 61 PYSPSPYDRR 71 in Ara h 2.02) were detected.…”

Section: Resultsmentioning

confidence: 96%

Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity

Apostolović

Stanić-Vučinić

Jongh

et al. 2016

Sci Rep

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Conglutins represent the major peanut allergens and are renowned for their resistance to gastro-intestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.

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Section: Resultsmentioning

confidence: 96%

Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity

Apostolović

Stanić-Vučinić

Jongh

et al. 2016

Sci Rep

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“…The IgE‐binding properties of the liquid phase from the digestion mixtures (control peanut sample [CPS] and digested peanut sample [DPS]), as well as standard defatted peanut extracts, were analysed using an inhibition ELISA. Standard defatted raw peanut extract was prepared according to the method reported by Radosavljevic et al with all patients (Table ). For more details, see .…”

Section: Methodsmentioning

confidence: 99%

Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides

Prodić¹,

Stanić-Vučinić

Apostolović

et al. 2018

Clin Experimental Allergy

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“…Then the resulting tryptic peptides were subjected to Size Exclusion Chromatography (SEC) (Radosavljevic et al, ) (LC‐20AT, Shimadzu) by using a Shodex PROTEIN KW‐802.5(8.0 × 300 mm) column, the component was eluted with 0.05 M PBS phosphate buffer at 28 °C. The proteins were eluted by gradient flow rate 0–0.6 ml/min.…”

Section: Methodsmentioning

confidence: 99%

Modification of the reaction system of Ara h 2 catalyzed by MTGase: Products and reaction conditions analysis

Zhao

Ren

et al. 2017

J Food Process Preserv

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Peanut (Arachis hypogaea) is listed among the eight major food allergens, in which Ara h 2 is the major allergen. The microbial transglutaminase (MTGase)‐catalyzed cross‐linking reaction reduces the allergenicity of Ara h 2. However, deamidation might occur and influence the cross‐linking reaction. In this work, native and reduced Ara h 2 were catalyzed by MTGase. In addition to intermolecular cross‐linking, intramolecular cross‐linking and deamidation were proven to occur simultaneously. Moreover, intramolecular cross‐linking sites were identified using mass spectrometry and the PLINK software. The reactions moved toward different directions because of different reduction conditions and different protein concentrations. Practical applications Cross‐linking is a common processing method used to improve the textural and functional properties of protein. Deamidation reaction might occur during processing and influence the cross‐linking reaction. The two types of reactions have a competitive relation, because both of them occur on glutamine residue. In Ara h 2 and MTGase system, protein concentration and reduction content influence the direction of reaction. The results can be applied to modify the reaction system of Ara h 2 catalyzed by MTGase. In addition, the relationship between structure and properties changes on Ara h 2 was discussed based on analysis of cross‐linking sites.

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Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases

Cited by 14 publications

References 22 publications

Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity

Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity

Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides

Modification of the reaction system of Ara h 2 catalyzed by MTGase: Products and reaction conditions analysis

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