Food allergy: A clinician’s criteria for including sera in a serum bank

Ballmer‐Weber, Barbara; Fernández-Rivas, M.

doi:10.1016/j.fct.2008.07.018

Cited by 10 publications

(3 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…by ELISA and/or immunoblotting), the allergic reactions in the patient (case history and recent confirmation clinical tests, including skin prick test and double-blind placebo-controlled food challenge), and a sufficiently high IgE titer (yet not derived from patients showing broad-spectrum reactivity, such as atopic dermatitis and lupus patients) (Ballmer- Weber and Fernandez-Rivas, 2008;Goodman, 2008). by ELISA and/or immunoblotting), the allergic reactions in the patient (case history and recent confirmation clinical tests, including skin prick test and double-blind placebo-controlled food challenge), and a sufficiently high IgE titer (yet not derived from patients showing broad-spectrum reactivity, such as atopic dermatitis and lupus patients) (Ballmer- Weber and Fernandez-Rivas, 2008;Goodman, 2008).…”

Section: Ige Binding Testsmentioning

confidence: 99%

Scientific Opinion on the assessment of allergenicity of GM plants and microorganisms and derived food and feed

2010

EFSA Journal

411

231

View full text Add to dashboard Cite

The weight-of-evidence, case-by-case approach is considered the most appropriate way of assessing the allergenicity of genetically modified (GM) food and feed. This scientific opinion discusses various aspects to increase the strength and accuracy of this approach, including the latest developments pertaining to clinical aspects of allergic reactions, structural aspects of GM food and feed and in silico approaches, as well as IgE binding studies and cell-based methods, profiling techniques and animal models. In this context, conclusions and recommendations are provided to update and complement current risk assessment strategies for the allergenicity assessment of newly expressed protein(s) and whole GM food and feed. In summary, it is recommended that with regard to the search for sequence homology and structural similarities, the local alignment method with a known allergen with a threshold of 35% sequence identity over a window of at least 80 amino acids is considered a minimal requirement. When IgE binding tests are considered necessary, e.g. when there is sequence homology and/or structure similarity with known allergens, the use of individual sera from allergic individuals rather than pooled sera is recommended. In addition to the pepsin resistance test, it is recommended that the resistance to digestion of the newly expressed proteins is evaluated using other in vitro digestibility tests mimicking physiological conditions of humans. Finally, when the recipient of the introduced gene is allergenic, in order to compare the allergenicty of the whole GM plant with that of its appropriate comparator(s), it is recommended that relevant characterised endogenous allergens are included in the comparative compositional analysis of the GM plant and its appropriate comparator(s). Proposals for the use of additional testing that may improve the weight-of-evidence approach and 1 On request of EFSA, Question No EFSA-Q-2005-125, adopted on 30 June 2010. 2 Panel members:

show abstract

Section: Ige Binding Testsmentioning

confidence: 99%

Scientific Opinion on the assessment of allergenicity of GM plants and microorganisms and derived food and feed

2010

EFSA Journal

411

231

View full text Add to dashboard Cite

show abstract

“…Already many studies on GM feeds have been documented regarding animal performance and health, as well as resultant food safety [reviewed by (Flachowsky et al 2005; Report of the EFSA GMO panel working group on Animal feeding trials 2008)]. The previous studies (Chowdhury et al 2003; Einspanier et al 2004; Lutz et al 2005) on the digestive fate of Cry1Ab protein from GM maize (events: Bt11 and Bt176) in ruminant gastrointestinal tract (GIT) revealed that the recombinant protein is degraded during digestion.…”

Section: Introductionmentioning

confidence: 99%

Degradation of Cry1Ab protein from genetically modified maize (MON810) in relation to total dietary feed proteins in dairy cow digestion

Paul¹,

Guertler²,

Wiedemann³

et al. 2009

Transgenic Res

View full text Add to dashboard Cite

To investigate the relative degradation and fragmentation pattern of the recombinant Cry1Ab protein from genetically modified (GM) maize MON810 throughout the gastrointestinal tract (GIT) of dairy cows, a 25 months GM maize feeding study was conducted on 36 lactating Bavarian Fleckvieh cows allocated into two groups (18 cows per group) fed diets containing either GM maize MON810 or nearly isogenic non-GM maize as the respective diet components. All cows were fed a partial total mixed ration (pTMR). During the feeding trial, 8 feed (4 transgenic (T) and 4 non-transgenic (NT) pTMR) and 42 feces (26 T and 18 NT) samples from the subset of cows fed T and NT diets, and at the end of the feeding trial, digesta contents of rumen, abomasum, small intestine, large intestine and cecum were collected after the slaughter of six cows of each feeding group. Samples were analyzed for Cry1Ab protein and total protein using Cry1Ab specific ELISA and bicinchoninic acid assay, respectively. Immunoblot analyses were performed to evaluate the integrity of Cry1Ab protein in feed, digesta and feces samples. A decrease to 44% in Cry1Ab protein concentration from T pTMR to the voided feces (9.40 versus 4.18 μg/g of total proteins) was recorded. Concentrations of Cry1Ab protein in GIT digesta of cows fed T diets varied between the lowest 0.38 μg/g of total proteins in abomasum to the highest 3.84 μg/g of total proteins in rumen. Immunoblot analysis revealed the extensive degradation of recombinant Cry1Ab protein into a smaller fragment of around 34 kDa in GIT. The results of the present study indicate that the recombinant Cry1Ab protein from MON810 is increasingly degraded into a small fragment during dairy cow digestion.

show abstract

“…Food allergy is a growing health concern worldwide, with an increasing prevalence attributed to food, genetic, and environmental factors. Food allergy affects approximately 1 to 3% of adult and 5 to 8% of children (Ballmer-Weber and Fernández-Rivas, 2008). Food allergy is an IgE-mediated or non-IgE-mediated immune reaction, caused by certain foods or food additives (Petruláková and Valík, 2015).…”

Section: Introductionmentioning

confidence: 99%

Evaluation of allergenicity of cow milk treated with enzymatic hydrolysis through a mouse model of allergy

Liang

Wang

Yang

et al. 2022

Journal of Dairy Science

View full text Add to dashboard Cite

Cow milk (CM) allergy is a worldwide concern. Currently, few studies have been performed on the immunoreactivity of CM and fewer still on the antigenicity of CM in vivo and in vitro. In this study, we assessed the potential allergenicity of enzymatically hydrolyzed CM using in vitro ELISA and oral sensitization and challenge of BALB/c mice. Alcalase-, Protamex-, and Flavourzyme-treated CM (all from Novozymes) diminished IgE binding capacity, with greatest reductions of 56.31%, 50.62%, and 56.45%, respectively. Allergic symptoms and levels of total IgG 1 were reduced, and allergic inflammation of the lung, jejunum, and spleen was relieved. Moreover, the numbers of CD8 + T and B220 + cells decreased, and the balance of CD4 + T/ CD8 + T cells was effectively regulated. These findings suggest that the potential allergenicity of CM was reduced by enzymatic hydrolysis, and our research will lay a solid foundation for developing high-quality hypoallergenic CM products.

show abstract

Food allergy: A clinician’s criteria for including sera in a serum bank

Cited by 10 publications

References 35 publications

Scientific Opinion on the assessment of allergenicity of GM plants and microorganisms and derived food and feed

Scientific Opinion on the assessment of allergenicity of GM plants and microorganisms and derived food and feed

Degradation of Cry1Ab protein from genetically modified maize (MON810) in relation to total dietary feed proteins in dairy cow digestion

Evaluation of allergenicity of cow milk treated with enzymatic hydrolysis through a mouse model of allergy

Contact Info

Product

Resources

About