scholarly journals Purification and Characterization of Pathogenesis Related Class 10 Panallergens

Foods ◽  
2019 ◽  
Vol 8 (12) ◽  
pp. 609 ◽  
Author(s):  
Jane K. McBride ◽  
Hsiaopo Cheng ◽  
Soheila J. Maleki ◽  
Barry K. Hurlburt
Keyword(s):  
Immunoglobulin E ◽  
Birch Pollen ◽  
Cross Reactivity ◽  
Oral Allergy Syndrome ◽  
Universal Method ◽  
Purification Method ◽  
Variable Binding ◽  
Pathogenesis Related ◽  
Immunocap Isac

Oral allergy syndrome (OAS) describes an allergic reaction where an individual sensitized by pollen allergens develops symptoms after eating certain foods. OAS is caused by cross-reactivity among a class of proteins ubiquitous in plants called pathogenesis related class 10 (PR-10) proteins. The best characterized PR-10 protein is Bet v 1 from birch pollen and its putative function is binding hydrophobic ligands. We cloned a subset of seven recombinant PR-10 proteins from pollens, peanuts, and hazelnuts and developed a standard purification method for them. Immunoglobulin E (IgE) binding of purified PR-10 proteins was analyzed by ImmunoCAP ISAC microarray and enzyme-linked immunosorbent assays (ELISAs) with sera from allergic patients. We investigated the binding activities of PR10s by testing 16 different ligands with each protein and compared their secondary structures using circular dichroism (CD). The PR-10s in this study had very similar CD spectra, but bound IgE with very different affinities. All seven proteins showed a similar pattern of binding to the polyphenol ligands (resveratrol, flavonoids, and isoflavones) and variable binding to other potential ligands (fatty acids, sterols, and plant hormones). We suggest our protocol has the potential to be a near-universal method for PR-10 purification that will facilitate further research into this important class of panallergens.

Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform

2008 ◽  
Vol 389 (4) ◽  
pp. 415-423 ◽  
Author(s):  
Susanne Riecken ◽  
Buko Lindner ◽  
Arnd Petersen ◽  
Uta Jappe ◽  
Wolf-Meinhard Becker
Keyword(s):  
Birch Pollen ◽  
Diagnostic Procedures ◽  
Cross Reactivity ◽  
Exchange Chromatography ◽  
Size Exclusion ◽  
Reactive Protein ◽  
Bet V 1 ◽  
Peanut Extract ◽  
Natural Counterpart

Abstract The peanut allergen Ara h 8 is an important allergen for birch pollen allergic patients because of the cross-reactivity to the homologous Bet v 1. As the existence of Ara h 8 has been shown at the cDNA level so far (AY328088) and the allergen has indirectly been detected as natural protein, it was the aim of our study to identify natural Ara h 8 in peanut extract and to develop a purification strategy. This was achieved using a unique combination of purification steps, including optimized extraction conditions, size exclusion and ion exchange chromatography and treatment of the interfering contaminants with iodo-acetic acid. A characterization of the protein by microsequencing showed discrepancies to the deduced amino acid sequence of AY328088. For this reason, we cloned and expressed a new Ara h 8 isoform from cDNA (EU046325). This IgE-reactive protein corresponds to the results of microsequencing, ESI-FTICR-MS and trypsin fingerprinting analysis of the authentic and purified nAra h 8. Apart from the ultimate use of recombinant allergens for diagnostic procedures, there is also a scientific need for the natural counterpart, as it represents an excellent reference point by which to compare protein characteristics and to standardize diagnostic and therapeutic allergens.

scholarly journals Crossreactive allergen-specific IgE in children with birch pollen allergic rhinitis

2017 ◽  
Vol 14 (2) ◽  
pp. 66-70
Author(s):  
P V Samoylikov ◽  
S A Mazurina ◽  
P I Gushchin ◽  
V B Gervazieva
Keyword(s):  
Allergic Rhinitis ◽  
Birch Pollen ◽  
Humoral Response ◽  
Specific Ige ◽  
Cross Reactivity ◽  
Oral Allergy Syndrome ◽  
Food Allergens ◽  
Homologous Proteins ◽  
Total Ige ◽  
Bet V 1

Objective. The aim of this study was to research a sIgE allergen profile of birch pollen and to evaluate a contribution of some homologous food allergens as well as latex allergen to the development of sensibility in allergic rhinitis (AR) / rhinoconjunctivitis patients, in focus of cross-reactivity and oral allergy syndrome.. Methods. Blood sera of 21 AR/rhinoconjunctivitis patients (at the age of 3 to 16) and 20 healthy persons without allergy symptoms were used. sIgE to birch pollen, soybean, latex, apple and celery as well as the total IgE levels were measured by the ImmunoCAP method (Phadia, Sweden) and the ELISA kits (Alkorbio, Russia). Results. We detected high total IgE levels, sIgE to allergens of birch pollen, apple, celery, as well as to recombinant allergens of birch Bet v 1, Bet v 2 and soybean - Gly m 4 in AR patients. Correlation analysis of IgE humoral response to homologous proteins showed the direct valid dependence between the sIgE levels to birch isoallergen Bet v 1 and soy isoallergen Gly m 4 (r=0,84; p

scholarly journals IgE cross-reactivity measurement of cashew nut, hazelnut and peanut using a novel IMMULITE inhibition method

2020 ◽  
Vol 58 (11) ◽  
pp. 1875-1883
Author(s):  
Shanna Bastiaan-Net ◽  
Manou R. Batstra ◽  
Nasrin Aazamy ◽  
Huub F.J. Savelkoul ◽  
Johanna P.M. van der Valk ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Clinical Symptoms ◽  
Birch Pollen ◽  
Seed Storage ◽  
Specific Ige ◽  
Cross Reactivity ◽  
Strong Inhibitor ◽  
Reactivity Measurement ◽  
Cashew Nut ◽  
Pathogenesis Related Protein

AbstractBackgroundTree nut-allergic individuals are often sensitised towards multiple nuts and seeds. The underlying cause behind a multi-sensitisation for cashew nut, hazelnut, peanut and birch pollen is not always clear. We investigated whether immunoglobulin E antibody (IgE) cross-reactivity between cashew nut, hazelnut and peanut proteins exists in children who are multi-allergic to these foods using a novel IMMULITE®-based inhibition methodology, and investigated which allergens might be responsible. In addition, we explored if an allergy to birch pollen might play a role in this co-sensitisation for cashew nut, hazelnut and peanut.MethodsSerum of five children with a confirmed cashew nut allergy and suffering from allergic symptoms after eating peanut and hazelnut were subjected to inhibition immunoassays using the IMMULITE® 2000 XPi. Serum-specific IgE (sIgE) to seed storage allergens and pathogenesis-related protein 10 (PR10) allergens were determined and used for molecular multicomponent allergen correlation analyses with observed clinical symptoms and obtained inhibition data.ResultsIgE cross-reactivity was observed in all patients. Hazelnut extract was a strong inhibitor of cashew nut sIgE (46.8%), while cashew nut extract was less able to inhibit hazelnut extract (22.8%). Peanut extract showed the least inhibition potency. Moreover, there are strong indications that a birch pollen sensitisation to Bet v 1 might play a role in the observed symptoms provoked upon ingestion of cashew nut and hazelnut.ConclusionsBy applying an adjusted working protocol, the IMMULITE® technology can be used to perform inhibition assays to determine the risk of sIgE cross-reactivity between very different food components.

scholarly journals Pollen-food allergy syndrome in children

2020 ◽  
Vol 63 (12) ◽  
pp. 463-468 ◽  
Author(s):  
You Hoon Jeon
Keyword(s):  
Food Allergy ◽  
Allergic Reaction ◽  
Pediatric Patients ◽  
Immunoglobulin E ◽  
Pollen Allergy ◽  
Heat Stability ◽  
Cross Reactivity ◽  
Oral Allergy Syndrome ◽  
Food Ingestion ◽  
Systemic Reactions

Pollen-food allergy syndrome (PFAS) is an immunoglobulin E-mediated immediate allergic reaction caused by cross-reactivity between pollen and the antigens of foods—such as fruits, vegetables, or nuts—in patients with pollen allergy. A 42.7% prevalence of PFAS in Korean pediatric patients with pollinosis was recently reported. PFAS is often called oral allergy syndrome because of mild symptoms such as itching, urticaria, and edema mainly in the lips, mouth, and pharynx that appear after food ingestion. However, reports of systemic reactions such as anaphylaxis have been increasing recently. This diversity in the degree of symptoms is related to the types of trigger foods and the characteristics of allergens, such as heat stability. When pediatric patients with pollen allergy are treated, attention should be paid to PFAS and an active effort should be made to diagnose it.

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