Analysis of the potential allergenicity of traditional apple cultivars by Multiplex Biochip-Based Immunoassay

Pasquariello, Maria Silvia; Palazzo, Paola; Tuppo, Lisa; Liso, Marina; Petriccione, Milena; Rega, Pietro; Tartaglia, Alfonso; Tamburrini, Maurizio; Alessandri, Claudia; Ciardiello, Maria Antonietta; Mari, Adriano

doi:10.1016/j.foodchem.2012.04.075

Cited by 18 publications

(23 citation statements)

References 28 publications

(33 reference statements)

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“…Protein extract was prepared from the dried powder of alfalfa using the protein extraction procedure developed for plant foods 11 with a few modifications. Briefly, 20 g of ground dried leaves were homogenized in a solution made with 80 mL of 0.5 mol L ‐1 sodium chloride (NaCl), 0.8 g of poly(vinylpolypyrrolidone), 2 mL of 0.125 mol L ‐1 ethylenediaminetetraacetic acid and 2.2 g of ascorbic acid dissolved in 25 mL of water and brought to pH 3.5 by addition of sodium hydroxide (NaOH).…”

Section: Methodsmentioning

confidence: 99%

“…For instance, it can be used to investigate immunological similarities between different molecules and also to detect possible allergens in a protein mixture, such as a food extract, by performing IgE inhibition test. In food allergen testing, multiplex systems that allow the analysis of a comprehensive panel of possible allergens in the proteome of a food extract are especially of value 11–13 . Pasquariello et al ., for example, have used IgE inhibition tests performed with the Single Point Highest Inhibition Achievable assay (SPHIAa) in combination with a multiplex biochip‐based immunoassay to analyse the allergen profiles of protein extracts from different apple cultivars 11 and to select potentially hypo‐ or hyper‐allergenic apple cultivars.…”

Section: Introductionmentioning

confidence: 99%

“…In food allergen testing, multiplex systems that allow the analysis of a comprehensive panel of possible allergens in the proteome of a food extract are especially of value 11–13 . Pasquariello et al ., for example, have used IgE inhibition tests performed with the Single Point Highest Inhibition Achievable assay (SPHIAa) in combination with a multiplex biochip‐based immunoassay to analyse the allergen profiles of protein extracts from different apple cultivars 11 and to select potentially hypo‐ or hyper‐allergenic apple cultivars. Similarly, the IgE inhibition with the SPHIAa method, combined with the allergen multiplex FABER test, was used to assess the cross‐reaction between a protein extract and individual allergens, namely the cypress pollen extract and the peach and cypress GRPs 12 …”

Section: Introductionmentioning

confidence: 99%

“…1) combines proteomics‐based protein identification, immunological investigations, bioinformatics 30 and data mining to gain biological insights useful to evaluate the presence of potential allergens in protein extract. The possible allergenicity of the leaf protein extract of M. sativa L was investigated by IgE‐binding inhibition test using the SPHIAa method 11,12,31,32 associated to FABER test 12 . FABER is a nanotechnology‐based multiplex in vitro serological test, which takes advantage of database and bioinformatics tools of the Allergome platform (http://www.allergome.org/) to analyze and store diagnostic and research data.…”

Section: Introductionmentioning

confidence: 99%

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Potential allergenicity of Medicago sativa investigated by a combined IgE‐binding inhibition, proteomics and in silico approach

et al. 2020

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BACKGROUNDAlfalfa (Medicago sativa L) is one of the most planted crops worldwide primarily used to feed animals. The use of alfalfa in human diet as sprouts, infusions and nutritional supplements is rapidly gaining popularity. Despite this, allergenicity assessment of this novel plant food is largely lacking.RESULTSHere, leaf protein extract of alfalfa was studied using a combined proteomics, Immunoglobulin E (IgE)‐binding inhibition assay and in silico approach to find potential allergens. We have identified and annotated 129 proteins using in‐gel digestion proteomics and Blast2Go suit. A search against COMPARE database, using the identified proteins as query sequences, revealed high similarity with several allergenic proteins. The Single Point Highest Inhibition Achievable assay (SPHIAa) performed on the multiplex FABER® allergy testing system confirmed the in silico results and showed some additional potential allergens. This approach allowed the detection of proteins in alfalfa leaves cross‐reacting with plant allergens from three different allergen families such as lipid transfer, thaumatin‐like and Bet v 1‐like protein families. In addition, the absence of structural determinants cross‐reacting with seed storage allergenic proteins and with animal allergens was recorded.CONCLUSIONThis study reports for the first time potential allergenic proteins in alfalfa. The results suggest that this plant food can be safely introduced, as a protein‐rich supplement, in the diet of patients allergic to animal food allergens. Allergic patients towards certain plant food allergens need to be careful about consuming alfalfa because they might have allergic symptoms. © 2020 Society of Chemical Industry

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Potential allergenicity of Medicago sativa investigated by a combined IgE‐binding inhibition, proteomics and in silico approach

et al. 2020

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“…More importantly, it frequently fails to detect specific IgE because the composition of the surrogate markers can be very variable (Giangrieco et al, 2012). This high variability makes it impossible to have standardized extracts with a constant allergen composition, since this may be influenced by several factors, such as differences among plant cultivars, post-harvest treatments, specific phenological stages, and extraction protocols (Ciardiello et al, 2009; Pasquariello et al, 2012). Molecule-based diagnosis may overcome all these drawbacks, given the possibility of detecting the specific IgE against individual allergenic molecules (Giangrieco et al, 2012; Ciardiello et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Plant-Made Bet v 1 for Molecular Diagnosis

et al. 2019

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Allergic disease diagnosis is currently experiencing a breakthrough due to the use of allergenic molecules in serum-based assays rather than allergen extracts in skin tests. The former methodology is considered a very innovative technology compared with the latter, since it is characterized by flexibility and adaptability to the patient’s clinical history and to microtechnology, allowing multiplex analysis. Molecular-based analysis requires pure allergens to detect IgE sensitization, and a major goal, to maintain the diagnosis cost-effective, is to limit their production costs. In addition, for the production of recombinant eukaryotic proteins similar to natural ones, plant-based protein production is preferred to bacterial-based systems due to its ability to perform most of the post-translational modifications of eukaryotic molecules. In this framework, Plant Molecular Farming (PMF) may be useful, being a production platform able to produce complex recombinant proteins in short time-frames at low cost. As a proof of concept, PMF has been exploited for the production of Bet v 1a, a major allergen associated with birch (Betula verrucosa) pollen allergy. Bet v 1a has been produced using two different transient expression systems in Nicotiana benthamiana plants, purified and used in a new generation multiplex allergy diagnosis system, the patient-Friendly Allergen nano-BEad Array (FABER). Plant-made Bet v 1a is immunoreactive, binding IgE and inhibiting IgE-binding to the Escherichia coli expressed allergen currently available in the FABER test, thus suggesting an overall similar though non-overlapping immune activity compared with the E. coli expressed form.

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Allergic identification for ginkgo kernel protein in guinea pigs

Yang

Fan

et al. 2016

Food Sci Biotechnol

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L. can cause allergic reactions when consumed. In this paper, an allergy test to guinea pig was investigated. Guinea pigs were sensitized with 50 mg/mL of ginkgo kernel protein orally on days 1, 3, and 5, and intraperitoneally challenged with 100mg/mL of the protein on day 7 after the last sensitization. The volume of sensitization and challenge was 0.20mL/100 g weight. The results showed the average allergy grade for guinea pigs reached four and the allergy rate was 100%. The immunoglobulin G and E levels in sera were significantly higher than those in the controls. Footpads swelled distinctly, and the passive cutaneous allergy test manifested a positive response. There were inflammatory changes in the lungs and intestines. In conclusion, the present results may indicate that gingko kernel protein has an allergenic capacity.

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Analysis of the potential allergenicity of traditional apple cultivars by Multiplex Biochip-Based Immunoassay

Cited by 18 publications

References 28 publications

Potential allergenicity of Medicago sativa investigated by a combined IgE‐binding inhibition, proteomics and in silico approach

Potential allergenicity of Medicago sativa investigated by a combined IgE‐binding inhibition, proteomics and in silico approach

Plant-Made Bet v 1 for Molecular Diagnosis

Allergic identification for ginkgo kernel protein in guinea pigs

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