Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional assays of allergenicity

Palmer, G William; Dibbern, Donald A.; Burks, A. Wesley; Bannon, Gary A.; Bock, S. Allan; Porterfield, Harry S.; McDermott, Robert; Dreskin, Stephen C.

doi:10.1016/j.clim.2005.02.011

Cited by 103 publications

(92 citation statements)

References 41 publications

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“…Rabbit IgG antihuman polyclonal IgE (Bethyl Laboratories, Inc, Montgomery, TX) was used as a positive control. 13 Results were expressed as the percentage of release from cells sensitized with individual serum minus spontaneous release (with buffer), which was then divided by total release with 1% Triton X-100 (Sigma-Aldrich, St. Louis, MO) as follows:…”

Section: Methodsmentioning

confidence: 99%

Effect of chemical modifications on allergenic potency of peanut proteins

Bencharitiwong

Kleij²,

Koppelman³

et al. 2015

allergy asthma proc

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Section: Methodsmentioning

confidence: 99%

Effect of chemical modifications on allergenic potency of peanut proteins

Bencharitiwong

Kleij²,

Koppelman³

et al. 2015

allergy asthma proc

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“…The IgE antibody reactivity to peanut allergens Ara h 1, Ara h 2, Ara h 3, Ara h 6, and Ara h 7 has recently been investigated in peanut-allergic patients using natural [18,19,20,21,22,23,24] or recombinant [25,26] allergens. In our previous study in a small cohort of patients, both SPT and immunological assays using recombinant major peanut allergens Ara h 1, Ara h 2, and Ara h 3 significantly increased the specificity and sensitivity of diagnosis [27].…”

Section: Introductionmentioning

confidence: 99%

A Novel Immunoassay Using Recombinant Allergens Simplifies Peanut Allergy Diagnosis

Codreanu¹,

Collignon²,

Roitel³

et al. 2010

Int Arch Allergy Immunol

127

101

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Background: Double-blind placebo-controlled food challenge (DBPCFC) is currently considered the gold standard for peanut allergy diagnosis. However, this procedure that requires the hospitalization of patients, mostly children, in specialized centers for oral exposure to allergens may cause severe reactions requiring emergency measures. Thus, a simpler and safer diagnosis procedure is needed. The aim of this study was to evaluate the diagnostic performance of a new set of in vitro blood tests for peanut allergy. Methods: The levels of IgE directed towards peanut extract and recombinant peanut allergens Ara h 1, Ara h 2, Ara h 3, Ara h 6, Ara h 7, and Ara h 8 were measured in 3 groups of patients enrolled at 2 independent centers: patients with proven peanut allergy (n = 166); pollen-sensitized subjects without peanut allergy (n = 61), and control subjects without allergic disease (n = 10). Results: Seventy-nine percent of the pollen-sensitized patients showed IgE binding to peanut, despite their tolerance to peanut. In contrast, combining the results of specific IgE to peanut extract and to recombinant Ara h 2 and Ara h 6 yielded a peanut allergy diagnosis with a 98% sensitivity and an 85% specificity at a positivity threshold of 0.10 kU/l. Use of a threshold of 0.23 kU/l for recombinant Ara h 2 increased specificity (96%) at the cost of sensitivity (93%). Conclusion: A simple blood test can be used to diagnose peanut allergy with a high level of precision. However, DBPCFC will remain useful for the few cases where immunological and clinical observations yield conflicting results.

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“…decrease viability) in the RBL cells (Ladics et al, 2008;Marchand et al, 2003). This toxicity appears to be due to naturally occurring xenoreactive antibodies (Palmera et al, 2005;Schuurman et al, 2003). Further, the optimal concentration for allergens or allergen extracts may also be important for inducing IgE-mediated responses with such cell lines.…”

Section: Rat Basophil Leukemia (Rbl) Cell Modelmentioning

confidence: 99%

“…Immunochemical methods depend on IgE that is present in allergen-specific polyclonal animal sera or human patient sera to bind to molecules bound to solid matrices like cellulose (enzyme allergosorbent test [EAST], Immuno-CAPs) or nitrocellulose (Western blotting). This binding to the matrix may change the structural integrity of the allergens and, thus, destroy the epitopes responsible for inducing allergy in vivo (Palmera et al, 2005;Vogel et al, 2005). Further, the results of immunochemical methods that are based on allergenspecific IgE are susceptible to a presence of IgG of the same specificity (Kadooka et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Use of a rat basophil leukemia (RBL) cell-based immunological assay for allergen identification, clinical diagnosis of allergy, and identification of anti-allergy agents for use in immunotherapy

Sun

Zhou

Zhou³

et al. 2014

Journal of Immunotoxicology

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(2015) Use of a rat basophil leukemia (RBL) cell-based immunological assay for allergen identification, clinical diagnosis of allergy, and identification of anti-allergy agents for use in immunotherapy, Journal of Immunotoxicology, 12:2, 199-205, DOI: 10.3109/1547691X.2014 AbstractFood allergy is an important public health problem that affects an estimated 8% of young children and 2% of adults. With an increasing interest in genetically-engineered foods, there is a growing need for development of sensitive and specific tests to evaluate potential allergenicity of foods and novel proteins as well as to determine allergic responses to ensure consumer safety. This review covers progress made in the field of development of cell models, specifically that involving a rat basophil leukemia (RBL) cell-based immunoassay, for use in allergen identification, diagnosis, and immunotherapy. The RBL assay has been extensively employed for determining biologically relevant cross-reactivities of food proteins, assessing the effect of processing on the allergenicity of food proteins, diagnosing allergic responses to whole-food products, and identifying anti-allergy food compounds. From the review of the literature, one might conclude the RBL cell-based assay is a better test system when compared to wild-type mast cell and basophil model systems for use in allergen identification, diagnosis, and analyses of potential immunotherapeutics. However, it is important to emphasize that this assay will only be able to identify those allergens to which the human has already been exposed, but will not identify a truly novel allergen, i.e. one that has never been encountered as in its preferred (humanized) configuration.

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Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional assays of allergenicity

Cited by 103 publications

References 41 publications

Effect of chemical modifications on allergenic potency of peanut proteins

Effect of chemical modifications on allergenic potency of peanut proteins

A Novel Immunoassay Using Recombinant Allergens Simplifies Peanut Allergy Diagnosis

Use of a rat basophil leukemia (RBL) cell-based immunological assay for allergen identification, clinical diagnosis of allergy, and identification of anti-allergy agents for use in immunotherapy

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