Comparative structural and thermal stability studies of Cuc m 2.0101, Art v 4.0101 and other allergenic profilins

Kapingidza, A. Brenda; Pye, Sarah; Hyduke, Noah; Dolamore, Coleman; Pote, Swanandi; Schlachter, Caleb R.; Commins, Scott P.; Kowal, Krzysztof; Chruszcz, M.

doi:10.1016/j.molimm.2019.07.004

Cited by 23 publications

(20 citation statements)

References 53 publications

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“…It is commonly accepted, however, that profilin-dependent allergic reactions to food result from cross-reactivity between pollen and food profilins where the former are true sensitizers [6,7]. Although some profilins can elicit adverse immune responses like anaphylaxis, the infrequent systemic reactions observed in patients after oral exposure to profilins is due to their low stability and high susceptibility to denaturation by proteases and the acidic environment in the digestive tract [9,10].…”

Section: Introductionmentioning

confidence: 99%

Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies

et al. 2020

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Four recombinant (r) allergens (rAmb a 8.0101, rArt v 4.0101, rBet v 2.0101, and rPhl p 12.0101) were successfully produced and used for sensitization studies. The allergens belong to the profilin family which is one of the most numerous allergen families. These four proteins represent allergens originating from pollen of weeds (rAmb a 8.0101 and rArt v 4.0101), tree (rBet v 2.0101) and grass (rPhl p 12.0101). The recombinant allergens were characterized using various biochemical and biophysical methods and tested for their ability to bind patient-derived antibodies. One hundred patients aged 2 to 50 years sensitized to pollen and plant-derived food allergens (IgE > 0.35 kU/L) were included. Sensitization to individual allergen sources and components of birch and timothy pollens was evaluated using multiparameter immunoblots. The presence of IgE to pollen-derived recombinant profilins rAmb a 8.0101, rArt v 4.0101, rBet v 2.0101, and rPhl p 12.0101 in serum was evaluated using ELISA method. The presence of IgE against pollen profilins was detected in 20 out of 100 studied patients. High correlation was seen between IgE ELISA results with individual pollen profilins. In summary, it was shown that the recombinant versions of the four allergenic profilins can be used for sensitization studies and for component-resolved allergy diagnostics.

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Section: Introductionmentioning

confidence: 99%

Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies

et al. 2020

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“…Profilins are heat‐labile proteins and they are easily degraded by the gastrointestinal proteases. Although the primary structure is highly conserved, profilins from different sources show some individual structural features, as also highlighted by the different melting temperatures reported for some of them deriving from grapevine, bell pepper, watermelon, hazel, muskmelon, soybean, apple, bean, cherry, almond, peach, tomato and potato [51 ].…”

Section: Class 2 Food Allergymentioning

confidence: 99%

“…Even more highly conserved than the amino acid sequence is the overall 3D‐structure of these proteins. In fact, their folding is found conserved even in profilins with a low sequence similarity and in phylogenetically distantly related, or unrelated, organisms [51, 52 ]. Therefore, the common co‐recognition between different profilins [53 ] can be related to a shared panel of IgE epitopes due to the conservation of sequence fragments and the overall folding [34 ].…”

Section: Class 2 Food Allergymentioning

confidence: 99%

Molecular approach to a patient’s tailored diagnosis of the oral allergy syndrome

Alessandri¹,

Ferrara²,

Bernardi³

et al. 2020

Clin Transl Allergy

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Oral allergy syndrome (OAS) is one of the most common IgE-mediated allergic reactions. It is characterized by a number of symptoms induced by the exposure of the oral and pharyngeal mucosa to allergenic proteins belonging to class 1 or to class 2 food allergens. OAS occurring when patients sensitized to pollens are exposed to some fresh plant foods has been called pollen food allergy syndrome (PFAS). In the wake of PFAS, several different associations of allergenic sources have been progressively proposed and called syndromes. Molecular allergology has shown that these associations are based on IgE co-recognition taking place between homologous allergens present in different allergenic sources. In addition, the molecular approach reveals that some allergens involved in OAS are also responsible for systemic reactions, as in the case of some food Bet v 1-related proteins, lipid transfer proteins and gibberellin regulated proteins. Therefore, in the presence of a convincing history of OAS, it becomes crucial to perform a patient's tailored molecule-based diagnosis in order to identify the individual IgE sensitization profile. This information allows the prediction of possible cross-reactions with homologous molecules contained in other sources. In addition, it allows the assessment of the risk of developing more severe symptoms on the basis of the features of the allergenic proteins to which the patient is sensitized. In this context, we aimed to provide an overview of the features of relevant plant allergenic molecules and their involvement in the clinical onset of OAS. The value of a personalized moleculebased approach to OAS diagnosis is also analyzed and discussed.

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“…Proteins that are involved in physiology related basic mechanisms are generally expressed in all plant species. One example is the profilin that is known to be expressed in all plant tissues 5 . Plant pathogenesis‐related Bet v 1‐like proteins (PR‐10) are also ubiquitous and considered panallergens 6 .…”

Section: Introductionmentioning

confidence: 99%

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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Comparative structural and thermal stability studies of Cuc m 2.0101, Art v 4.0101 and other allergenic profilins

Cited by 23 publications

References 53 publications

Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies

Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies

Molecular approach to a patient’s tailored diagnosis of the oral allergy syndrome

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

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