Protein Allergens, Toxins, and Bioinformatics (PATB) Committee

 

Protein Allergens, Toxins, and Bioinformatics (PATB) Committee

Mission Statement

The PATB is committed to advancing the scientific understanding of the relevant parameters defining allergenic proteins and protein toxins, and to encourage the development of reliable and accurate methodologies for characterizing the allergenic potential of novel proteins in order to leverage the potential of bioinformatics approaches in accomplishing these efforts.

Renaming the Committee: PATC to PATB

Formerly the Protein Allergenicity Technical Committee (PATC), the Committee has adopted a new designation (Protein Allergens, Toxins and Bioinformatics [PATB] Committee) to embrace a broader scope, expertise, interests, and collaborators in the fields of bioinformatics and protein toxins, while strengthening its core focus in allergenicity.

Committee Contacts

HESI Staff

Lucilia Mouries, PhD
lmouries@hesiglobal.org

Leadership Team

Antonella Cianferoni, MD, PhD
The Children's Hospital of Pennsylvania,
University of Pennsylvania

Emir Islamovic, PhD
BASF Agricultural Solutions Seed LLC

Ronald van Ree, PhD
Academic Medical Center, University of Amsterdam

Members and Fact Sheet

Committee Events

HESI PATC and IFBiC Biotechnology Update Symposium 2013

Arlington, Virginia, USA

The 7-8 May 2013 Biotechnology Update Symposium in Arlington, VA, was co-sponsored by the HESI Protein Allergenicity Technical Committee (PATC) and the ILSI International Food Biotechnology Committee (IFBiC).

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HESI Workshop on “Food Allergy and Safety Assessment”

Beijing, China

The 15-16 April 2013 Food Allergy and Safety Assessment Workshop in Beijing, China, was co-sponsored by the HESI Protein Allergenicity Technical Committee, the ILSI Focal Point in China, the ILSI International Food Biotechnology Committee (IFBiC), the China National Center for Food Safety Risk Assessment, and the China Key Laboratory on Food Safety Risk Assessment of the Ministry of Health.

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Committee Publications

All Publications

Protease resistance of food proteins: a mixed picture for predicting allergenicity but a useful tool for assessing exposure

Susceptibility to pepsin digestion of candidate transgene products is regarded an important parameter in the weight-of-evidence approach for allergenicity risk assessment of genetically modified crops. It has been argued that protocols used for this assessment should better reflect physiological conditions encountered in representative food consumption scenarios.

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Variation in Seed Allergen Content From Three Varieties of Soybean Cultivated in Nine Different Locations in Iowa, Illinois, and Indiana

Soybean (Glycine max) is an important food stock, and also considered an allergenic food with at least eight well characterized allergens. However, it is a less prevalent allergen source than many other foods and is rarely life-threatening. Soybean is incorporated into commonly consumed foods, and therefore, the allergens pose a potential concern for individuals already sensitized. The protein profile of soybean can be affected by several factors including genetic and environmental. To investigate how soybean allergen content may be affected by genetics and/or environment, nine soy allergens were quantified from three commercial soybean varieties grown at nine locations in three states within a single climate zone in North America; Iowa, Illinois, and Indiana, United States. Quantitation was achieved using liquid chromatography-selected reaction monitoring (LC-SRM) tandem mass spectrometry with AQUA peptide standards specific to the nine target allergens.

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Functional classification of protein toxins as a basis for bioinformatic screening

Proteins are fundamental to life and exhibit a wide diversity of activities, some of which are toxic. Therefore, assessing whether a specific protein is safe for consumption in foods and feeds is critical. Simple BLAST searches may reveal homology to a known toxin, when in fact the protein may pose no real danger.

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Inter-laboratory optimization of protein extraction, separation, and fluorescent detection of endogenous rice allergens

In rice, several allergens have been identified such as the non-specific lipid transfer protein-1, the α-amylase/trypsin-inhibitors, the α-globulin, the 33 kDa glyoxalase I (Gly I), the 52–63 kDa globulin, and the granule-bound starch synthetase. The goal of the present study was to define optimal rice extraction and detection methods that would allow a sensitive and reproducible measure of several classes of known rice allergens. In a three-laboratory ring-trial experiment, several protein extraction methods were first compared and analyzed by 1D multiplexed SDS-PAGE. In a second phase, an inter-laboratory validation of 2D-DIGE analysis was conducted in five independent laboratories, focusing on three rice allergens (52 kDa globulin, 33 kDa glyoxalase I, and 14–16 kDa α-amylase/trypsin inhibitor family members). The results of the present study indicate that a combination of 1D multiplexed SDS-PAGE and 2D-DIGE methods would be recommended to quantify the various rice allergens.

Please click here to view this open access publication.

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Assessment of potential adjuvanticity of Cry proteins

Genetically modified (GM) crops have achieved success in the marketplace and their benefits extend beyond the overall increase in harvest yields to include lowered use of insecticides and decreased carbon dioxide emissions. The most widely grown GM crops contain gene/s for targeted insect protection, herbicide tolerance, or both. Plant expression of Bacillus thuringiensis (Bt) crystal (Cry) insecticidal proteins have been the primary way to impart insect resistance in GM crops. Although deemed safe by regulatory agencies globally, previous studies have been the basis for discussions around the potential immuno-adjuvant effects of Cry proteins. These studies had limitations in study design. The studies used animal models with extremely high doses of Cry proteins, which when given using the ig route were co-administered with an adjuvant. Although the presumption exists that Cry proteins may have immunostimulatory activity and therefore an adjuvanticity risk, the evidence shows that Cry proteins are expressed at very low levels in GM crops and are unlikely to function as adjuvants. This conclusion is based on critical review of the published literature on the effects of immunomodulation by Cry proteins, the history of safe use of Cry proteins in foods, safety of the Bt donor organisms, and pre-market weight-of-evidence-based safety assessments for GM crops.

Read more

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