Quality Control of Biomedicinal Allergen Products – Highly Complex Isoallergen Composition Challenges Standard MS Database Search and Requires Manual Data Analyses

Spiric, Jelena; Engin, Anna M.; Karas, Michael; Reuter, Andreas

doi:10.1371/journal.pone.0142404

Cited by 29 publications

(54 citation statements)

References 35 publications

(46 reference statements)

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“…New York, NC. The identity of the protein was confirmed by in‐gel digestion followed by LC/MS analysis according to with slight modifications as specified in …”

Section: Methodsmentioning

confidence: 99%

“…NewYork, NC. The identity of the protein was confirmed by in-gel digestion followed by LC/MS analysis according to25 with slight modifications as specified in 26. 2.4 | IgE-binding and cross-reactivity assaysSpecific IgE values were determined by using experimental Immuno-CAP 27 for rTri tu 14 and commercially available ImmunoCAPs for rTri a 14.01 (f433), rPru p 3 (f420), and T. aestivum wheat (f4) (Thermo Fisher Scientific).…”

mentioning

confidence: 99%

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Identification and molecular characterization of allergenic non‐specific lipid‐transfer protein from durum wheat (Triticum turgidum)

Safi

Wangorsch

Lidholm

et al. 2018

Clin Experimental Allergy

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“…New York, NC. The identity of the protein was confirmed by in‐gel digestion followed by LC/MS analysis according to with slight modifications as specified in …”

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Identification and molecular characterization of allergenic non‐specific lipid‐transfer protein from durum wheat (Triticum turgidum)

Safi

Wangorsch

Lidholm

et al. 2018

Clin Experimental Allergy

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“…In addition, they reported on a set of reference mAb that were fivefold less sensitive to the reference allergen Bet v 1.0101 than to Bet v 1 in natural extracts. At the Paul‐Ehrlich Institute, we demonstrated that natural birch pollen extract includes a mixture of isoforms, at least 18 different sequence variants of Bet v 1, including an isoallergen that had not been previously been detected at the protein level . Having identified these issues, the ELISA assays for Bet v 1 were fully characterized in 2012 and validated in 2016 .…”

Section: Standardization Of Allergenic Extractsmentioning

confidence: 99%

Mass spectrometry to complement standardization of house dust mite and other complex allergenic extracts

Spiric¹,

Reuter

Rabin³

2017

Clin Experimental Allergy

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In the United States, the Center for Biologics Evaluation and Research of the US Food and Drug Administration regulates biologics used for diagnosis and treatment of allergic diseases. The Code of Federal Regulations 21CFR680.3(e) states that when measured, the potency of an allergenic extract is assessed according to its allergenic activity. As of 2016, 19 allergenic extracts are standardized for potency in the United States. While these standardized extracts constitute a minority of those available, they treat the most prevalent allergies (e.g. grass and ragweed pollens, dust mites, and cat) and those that induce life-threatening anaphylaxis (e.g. Hymenoptera venom). Standardization for potency enhances safety and efficacy of immunotherapy by minimizing the risks of variations in allergen dosing when switching from one lot of manufactured extract to another, and by providing an objective measure of stability of each lot of allergenic extract over time. Allergenic extracts that have multiple immunodominant allergenic proteins are standardized with little or no information about compositional differences among extracts. Here, we propose application of mass spectrometry towards measurement of compositional differences among extracts that may affect the efficacy and safety of allergen immunotherapy. In addition, we discuss of house dust mite allergen extracts as a prototypical complex extract that may be standardized by mass spectrometry.

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“…For purified natural and recombinant proteins the level of purity needs to be determined and additional protein contaminations with and without allergenic activity identified. Also the range of potential isoforms with varying IgE binding capacity needs to be defined as a reference set of proteins . Especially for recombinant proteins lipopolysaccharide (LPS) contamination should be ruled out since this could affect further immunization/sensitization studies.…”

Section: Introductionmentioning

confidence: 99%

Current (Food) Allergenic Risk Assessment: Is It Fit for Novel Foods? Status Quo and Identification of Gaps

Mazzucchelli

Holzhauser

Veličković

et al. 2017

Molecular Nutrition Food Res

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Food allergies are recognized as a global health concern. In order to protect allergic consumers from severe symptoms, allergenic risk assessment for well‐known foods and foods containing genetically modified ingredients is installed. However, population is steadily growing and there is a rising need to provide adequate protein‐based foods, including novel sources, not yet used for human consumption. In this context safety issues such as a potential increased allergenic risk need to be assessed before marketing novel food sources. Therefore, the established allergenic risk assessment for genetically modified organisms needs to be re‐evaluated for its applicability for risk assessment of novel food proteins. Two different scenarios of allergic sensitization have to be assessed. The first scenario is the presence of already known allergenic structures in novel foods. For this, a comparative assessment can be performed and the range of cross‐reactivity can be explored, while in the second scenario allergic reactions are observed toward so far novel allergenic structures and no reference material is available. This review summarizes the current analytical methods for allergenic risk assessment, highlighting the strengths and limitations of each method and discussing the gaps in this assessment that need to be addressed in the near future.

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Quality Control of Biomedicinal Allergen Products – Highly Complex Isoallergen Composition Challenges Standard MS Database Search and Requires Manual Data Analyses

Cited by 29 publications

References 35 publications

Identification and molecular characterization of allergenic non‐specific lipid‐transfer protein from durum wheat (Triticum turgidum)

Identification and molecular characterization of allergenic non‐specific lipid‐transfer protein from durum wheat (Triticum turgidum)

Mass spectrometry to complement standardization of house dust mite and other complex allergenic extracts

Current (Food) Allergenic Risk Assessment: Is It Fit for Novel Foods? Status Quo and Identification of Gaps

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