The Effector Function of Allergens

Hazebrouck, Stéphane; Canon, Nicole; Dreskin, Stephen C.

doi:10.3389/falgy.2022.818732

Cited by 9 publications

(6 citation statements)

References 105 publications

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“…VLP-Complex administration altered this serological profile, by significantly reducing sIgG2a levels in allergic specimens in almost a two-fold ratio ( Figure 5D ). We also observed a downward tendency in sIgE levels (P = 0.06), the most well-known biomarker associated with allergic symptomatology ( 52 ) ( Figure 5B ), although anti-Pru p 3 sIgG1 remained unaltered ( Figure 5C ).…”

Section: Resultsmentioning

confidence: 67%

Suitability of potyviral recombinant virus-like particles bearing a complete food allergen for immunotherapy vaccines

Pazos-Castro

Margain²,

González-Klein³

et al. 2022

Front. Immunol.

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Virus-like particles (VLPs) have been gaining attention as potential platforms for delivery of cargos in nanomedicine. Although animal viruses are largely selected due to their immunostimulatory capacities, VLPs from plant viruses constitute a promising alternative to be considered. VLPs derived from Turnip mosaic virus (TuMV) have proven to present a tridimensional structure suited to display molecules of interest on their surface, making them interesting tools to be studied in theragnostic strategies. Here, we study their potential in the treatment of food allergy by genetically coupling TuMV-derived VLPs to Pru p 3, one of the most dominant allergens in Mediterranean climates. VLPs-Pru p 3 were generated by cloning a synthetic gene encoding the TuMV coat protein and Pru p 3, separated by a linker, into a transient high-expression vector, followed by agroinfiltration in Nicotiana benthamiana plants. The generated fusion protein self-assembled in planta to form the VLPs, which were purified by exclusion chromatography. Their elongated morphology was confirmed by electron microscopy and their size (~400 nm), and monodispersity was confirmed by dynamic light scattering. Initial in vitro characterization confirmed that they were able to induce proliferation of human immune cells. This proliferative capability was enhanced when coupled with the natural lipid ligand of Pru p 3. The resultant formulation, called VLP-Complex, was also able to be transported by intestinal epithelial cells, without affecting the monolayer integrity. In light of all these results, VLP-Complex was furtherly tested in a mouse model of food allergy. Sublingual administration of VLP-Complex could effectively reduce some serological markers associated with allergic responses in mice, such as anti-Pru p 3 sIgE and sIgG2a. Noteworthy, no associated macroscopic, nephritic, or hepatic toxicity was detected, as assessed by weight, blood urea nitrogen (BUN) and galectin-3 analyses, respectively. Our results highlight the standardized production of allergen-coated TuMV-VLPs in N. benthamiana plants. The resulting formula exerts notable immunomodulatory properties without the need for potentially hazardous adjuvants. Accordingly, no detectable toxicity associated to their administration was detected. As a result, we propose them as good candidates to be furtherly studied in the treatment of immune-based pathologies.

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Section: Resultsmentioning

confidence: 67%

Suitability of potyviral recombinant virus-like particles bearing a complete food allergen for immunotherapy vaccines

Pazos-Castro

Margain²,

González-Klein³

et al. 2022

Front. Immunol.

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“…Importantly, while the sELISA requires two spatially separated binding epitopes for capture and detection antibodies, the cELISA only needs one binding site, possibly leading to a lower detected BLG residue content by sELISA compared to cELISA. 48 However, since allergenic fragments need two IgE epitopes to cross-link IgE/IgE receptor complexes on mast cells and basophils to release activity mediators, 49 sELISA is more suitable for allergen allergenicity evaluation. "μg/mL" was used for UHT milk, yoghurt samples, and beverage; "μg/g" was used for bread and cookie.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

One-Step Purification of IgE Epitope-Specific Antibody Using Immunomagnetic Beads and Highly Sensitive Detection of Bovine β-Lactoglobulin for the Prediction of Milk Allergenicity in Foods

He,

Xiong,

et al. 2023

J. Agric. Food Chem.

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Bovine β-lactoglobulin (BLG) is a common allergen found in milk, and the immunoglobulin E (IgE) epitope plays a crucial role in cow milk allergy. Therefore, targeting the IgE epitope could be useful in accurately detecting BLG and assessing its allergenicity. However, producing an IgE epitope-specific antibody (IgE-EsAb) through traditional methods requires complex and time-consuming procedures. Here, IgE-EsAb was purified from rabbit anti-BLG sera by immunomagnetic beads in one step. Then, a sandwich ELISA (sELISA) based on the IgE-EsAb was developed to detect BLG and predict the potential milk allergenicity in foods. The obtained IgE-EsAb could specifically recognize the target IgE epitope of BLG and exhibited high affinity and specificity. The developed IgE-EsAb-based sELISA demonstrated an ultra-wide linear range of 3.9–1.28 × 105 ng/mL, with a limit of detection of 0.49 ng/mL for BLG. Additionally, the proposed immunoassay showed high specificity and recoveries (91.24–109.61%). The ability of the IgE-EsAb-based sELISA to evaluate the potential milk allergenicity in foods was validated using sera from cow milk allergy patients. These results suggest that immunomagnetic beads are an effective tool for rapidly obtaining the IgE-EsAb, and our proposed sELISA could be a reliable and user-friendly method for monitoring trace amounts of BLG and predicting the potential milk allergenicity of food samples.

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“…Clearly, the multiplex allergen microarray-based system is an in vitro test that allows the detection of allergenic proteins and the assessment of their recognition by a specific IgE. However, the assessment of IgE binding is not proof that a protein will really cause an allergic reaction in sensitized patients [ 105 ]. The assessment of IgE binding provides useful indications, but when testing the effectiveness of processing methods in the reduction of allergenicity, patient safety requires that the results must always be confirmed by in vivo tests.…”

Section: Discussionmentioning

confidence: 99%

Detection of Allergenic Proteins in Foodstuffs: Advantages of the Innovative Multiplex Allergen Microarray-Based Immunoassay Compared to Conventional Methods

Tuppo

Giangrieco

Tamburrini

et al. 2022

Foods

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Several factors can affect the allergen content and profile of a specific food, including processing procedures often leading to a decrease in allergenicity, although no change, or even an increase, have also been reported. Evaluation of the effectiveness of a processing procedure requires the availability of reliable methodologies to assess the variation in molecules able to induce allergic reactions in the analyzed food. Conventional and innovative strategies and methodologies can be exploited to identify allergenic proteins in foodstuffs. However, depending on the specific purposes, different methods can be used. In this review, we have critically reviewed the advantages of an innovative method, the multiplex allergen microarray-based immunoassay, in the detection of allergens in foodstuffs. In particular, we have analyzed some studies reporting the exploitation of an IgE-binding inhibition assay on multiplex allergen biochips, which has not yet been reviewed in the available literature. Unlike the others, this methodology enables the identification of many allergenic proteins, some of which are still unknown, which are recognized by IgE from allergic patients, with a single test. The examined literature suggests that the inhibition test associated with the multiplex allergen immunoassay is a promising methodology exploitable for the detection of IgE-binding proteins in food samples.

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The Effector Function of Allergens

Cited by 9 publications

References 105 publications

Suitability of potyviral recombinant virus-like particles bearing a complete food allergen for immunotherapy vaccines

Suitability of potyviral recombinant virus-like particles bearing a complete food allergen for immunotherapy vaccines

One-Step Purification of IgE Epitope-Specific Antibody Using Immunomagnetic Beads and Highly Sensitive Detection of Bovine β-Lactoglobulin for the Prediction of Milk Allergenicity in Foods

Detection of Allergenic Proteins in Foodstuffs: Advantages of the Innovative Multiplex Allergen Microarray-Based Immunoassay Compared to Conventional Methods

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