In vitro evaluation of digestive and endolysosomal enzymes to cleave <scp>CML</scp>‐modified Ara h 1 peptides

Mattison, Christopher P.; Dinter, Jens; Berberich, Matthew J.; Chung, Si-Yin; Reed, Shawndrika; Gall, Sylvie Le; Grimm, Casey C.

doi:10.1002/fsn3.215

Cited by 6 publications

(10 citation statements)

References 76 publications

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“…Cashew extract samples were prepared and characterized by LC–MS/MS in a manner similar to that described in previous work [27] . However, in these experiments equivalent amounts of protein (50 ng) from raw or roasted cashew nuts were digested with 0.2 ng trypsin, and samples were acidified with formic acid before being analyzed with an Agilent 1200 LC system, an Agilent Chip Cube interface, and an Agilent 6520 Q-TOF tandem mass spectrometer (Agilent Technologies, Santa Clara, CA, USA).…”

Section: Methodsmentioning

confidence: 99%

Heat-induced alterations in cashew allergen solubility and IgE binding

Mattison

Bren‐Mattison²,

Vant-Hull³

et al. 2016

Toxicology Reports

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Cashew nuts are an increasingly common cause of food allergy. We compare the soluble protein profile of cashew nuts following heating. SDS-PAGE indicate that heating can alter the solubility of cashew nut proteins. The 11S legumin, Ana o 2, dominates the soluble protein content in ready to eat and mildly heated cashew nuts. However, we found that in dark-roasted cashew nuts, the soluble protein profile shifts and the 2S albumin Ana o 3 composes up to 40% of the soluble protein. Analysis of trypsin-treated extracts by LC/MS/MS indicate changes in the relative number and intensity of peptides. The relative cumulative intensity of the 5 most commonly observed Ana o 1 and 2 peptides are altered by heating, while those of the 5 most commonly observed Ana o 3 peptides remaine relatively constant. ELISA experiments indicate that there is a decrease in rabbit IgG and human serum IgE binding to soluble cashew proteins following heating. Our findings indicate that heating can alter the solubility of cashew allergens, resulting in altered IgE binding. Our results support the use of both Ana o 2 and Ana o 3 as potential cashew allergen diagnostic targets.

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Section: Methodsmentioning

confidence: 99%

Heat-induced alterations in cashew allergen solubility and IgE binding

Mattison

Bren‐Mattison²,

Vant-Hull³

et al. 2016

Toxicology Reports

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“…Most of these assays have been used as excellent tools to evaluate the effect of different physicochemical properties on the IgE-binding capacity of plant food allergens (Table 2). Based on their simplicity and relative low cost, immunoblotting, ELISA and RAST/EAST/immunoCAP, using the serum/plasma from sensitised/allergic subjects, are the first-line assays, being applied to allergens from almost all plant families [88][89][90][91][92][93][94][95][96][97][98][99]. They are followed by the cellular ex vivo or in vitro cellular assays, which have also been widely employed to study the influence of physicochemical characteristics on protein allergenicity in most plant families [45,91,.…”

Section: Measuring the Effect On Allergenicitymentioning

confidence: 99%

Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?

Costa

Villa

Verhoeckx

et al. 2020

Clinic Rev Allerg Immunol

131

110

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This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Furthermore, data on physicochemical characteristics translating into clinical effects are limited, mainly because most studies are focused on in vitro IgE-binding. Clinical data assessing how these parameters affect the development and clinical manifestation of allergies is minimal, with only few reports evaluating the sensitising capacity of modified proteins (addressing different physicochemical properties) in murine allergy models. In vivo testing of modified pure proteins by SPT or DBPCFC is scarce. At this stage, a systematic approach to link the physicochemical properties with clinical plant allergenicity in real life scenarios is still missing.

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“…For example, heating milk or egg proteins can reduce IgE binding to some allergens, whereas heating cashew nuts or peanuts can alter allergen solubility. , In the presence of glucose or oxidizing agents, chemical modifications may alter the relative abundance of some peptides, as detected by LC-MS/MS, in hazelnut extracts . Similarly, nonenzymatic modification of lysine or arginine residues can destroy protease sites, thereby preventing cleavage by some proteases and potentially increasing the stability of allergens and other proteins . In some cases, such as egg and milk allergies, there is clear evidence that heating these foods in a wheat matrix decreases allergenicity in affected individuals. , Efforts have been invested in identifying and characterizing processing-induced modifications in peanut and tree nut allergens and correlating their effect(s) on the immunological properties of seed storage proteins …”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of Ana o 3 Modifications on Arginine-111 Residue in Heated Cashew Nuts

Mattison

Grimm

et al. 2017

J. Agric. Food Chem.

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Raw and roasted cashew nut extracts were evaluated for protein modifications by mass spectrometry. Independent modifications on the Arg-111 residue of Ana o 3 were observed in roasted but not raw cashew nuts. The mass changes of 72.0064 or 53.9529 Da are consistent with the formation of carboxyethyl and hydroimidazolone modifications at the Arg-111 residue. These same modifications were observed in Ana o 3 purified from roasted but not raw cashew nuts, albeit at a relatively low occurrence. Circular dichroism indicated that Ana o 3 purified from raw and roasted cashew nuts had similar secondary structure, and dynamic light scattering analysis indicated there was no observable difference in particle size. The stability of Ana o 3 purified from raw and roasted cashew nuts to trypsin was similar in the absence of or following treatment with a reducing agent. Only minor differences in IgE binding to Ana o 3 were observed by ELISA among a cohort of cashew-allergic patient sera.

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In vitro evaluation of digestive and endolysosomal enzymes to cleave CML‐modified Ara h 1 peptides

Cited by 6 publications

References 76 publications

Heat-induced alterations in cashew allergen solubility and IgE binding

Heat-induced alterations in cashew allergen solubility and IgE binding

Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?

Identification and Characterization of Ana o 3 Modifications on Arginine-111 Residue in Heated Cashew Nuts

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