Protein Allergens, Toxins, and Bioinformatics (PATB) Committee
Protein Allergens, Toxins, and Bioinformatics (PATB) Committee
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.
Greg Ladics, PhD
E.I. DuPont de Nemours and Company
Scott McClain, PhD
Ronald van Ree, PhD
Academic Medical Center, Amsterdam University
Members and Fact Sheet
The Health and Environmental Sciences Institute (HESI) Protein Allergens, Toxins, and Bioinformatics (PATB) Committee will be hosting a webinar to discuss emerging opportunities and innovations in the biotechnology and food safety assessment arenas. Learn more!
- Date: Wednesday, May 22, 2019
- Time: 11 AM - 12:30 PM EST
- Registration: Click here to register.
- Scott McClain, Regulatory Product Safety Scientist, Syngenta Crop Protection (USA), PATB Committee Co-Chair
- Lars Poulsen, Head of Research, Allergy Clinic, Copenhagen University Hospital at Gentofte (Denmark), Member of the COMPARE Database Peer-Review Expert Panel
Advances in agricultural and food biotechnology bring the opportunity to improve the way we grow food and feed crops. As part of the requirements to ensure food safety, it is vital to mitigate potential risks of introducing new allergens or unintended components in the food chain that could induce adverse reactions in humans.
The Health and Environmental Sciences Institute (HESI) Protein Allergens, Toxins, and Bioinformatics (PATB) committee engages international collaborative teams of academics, clinicians, regulators, and industry scientists who conduct research, design and populate public database resources, and convene trainings on the use and evaluation of biotechnology products. The PATB oversees the creation, maintenance, and distribution of the Comprehensive Protein Allergen Resource (COMPARE) Database whose use in conjunction bioinformatic tools, offers an effective means for assessing allergenic potential of novel food proteins.
Webinar attendees will:
- Learn directly from experts in the committee about the nuts and bolts of food safety assessment of biotechnology products, the committee contributions to the field and new emerging issues
- Engage in an interactive discussion about emerging opportunities, challenges, and innovations in the biotechnology and food safety assessment arenas
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.
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.
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.
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.
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.