The relevance of a digestibility evaluation in the allergenicity risk assessment of novel proteins. Opinion of a joint initiative of COST action ImpARAS and COST action INFOGEST

Verhoeckx, Kitty; Bøgh, Katrine Lindholm; Dupont, Didier; Egger, Lotti; Gadermaier, Gabriele; Larré, Colette; Mackie, Alan; Ménard, Olivia; Adel‐Patient, Karine; Picariello, Gianluca; Portmann, Reto; Smit, Joost J.; Turner, Paul J.; Untersmayr, Eva; Epstein, Michelle M.

doi:10.1016/j.fct.2019.04.052

Cited by 61 publications

(42 citation statements)

References 187 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The relationship between allergenicity and stability to digestion of a protein is still controversial due to a lack of knowledge on the exact route of exposure and mechanisms behind food sensitisation and food allergy. 1,24 For this reason, it is of paramount importance to further investigate the behaviour of known allergens during digestion and identify the products of digestion extensively. In the present study, SDS-PAGE was used to identify intact protein or protein fragments larger than 5 kDa in digesta samples of isolated proteins and meals.…”

Section: Introductionmentioning

confidence: 99%

The pattern of peptides released from dairy and egg proteins is highly dependent on the simulated digestion scenario

et al. 2020

Self Cite

View full text Add to dashboard Cite

show abstract

Section: Introductionmentioning

confidence: 99%

The pattern of peptides released from dairy and egg proteins is highly dependent on the simulated digestion scenario

et al. 2020

Self Cite

View full text Add to dashboard Cite

show abstract

“…With more than 30% of the population affected, immunoglobulin-E-mediated allergy is the most frequent immune disorder worldwide (Valenta, 2002;Valenta et al, 2010;Curin et al, 2018). Still, the determinants of what makes a protein an allergen are largely unknown (Scheurer et al, 2015;Verhoeckx et al, 2019). It has been demonstrated repeatedly that proteins with substantial similarity in sequence and structure are able to trigger an entirely different immune response (Mitropoulou et al, 2018;Eichhorn et al, 2019;Seutter von Loetzen et al, 2019;Tscheppe et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

Dynamics Rationalize Proteolytic Susceptibility of the Major Birch Pollen Allergen Bet v 1

Kamenik

Hofer

Handle

et al. 2020

Front. Mol. Biosci.

View full text Add to dashboard Cite

Proteolytic susceptibility during endolysosomal degradation is decisive for allergic sensitization. In the major birch pollen allergen Bet v 1 most protease cleavage sites are located within its secondary structure elements, which are inherently inaccessible to proteases. The allergen thus must unfold locally, exposing the cleavage sites to become susceptible to proteolysis. Hence, allergen cleavage rates are presumed to be linked to their fold stability, i.e., unfolding probability. Yet, these locally unfolded structures have neither been captured in experiment nor simulation due to limitations in resolution and sampling time, respectively. Here, we perform classic and enhanced molecular dynamics (MD) simulations to quantify fold dynamics on extended timescales of Bet v 1a and two variants with higher and lower cleavage rates. Already at the nanosecond-timescale we observe a significantly higher flexibility for the destabilized variant compared to Bet v 1a and the proteolytically stabilized mutant. Estimating the thermodynamics and kinetics of local unfolding around an initial cleavage site, we find that the Bet v 1 variant with the highest cleavage rate also shows the highest probability for local unfolding. For the stabilized mutant on the other hand we only find minimal unfolding probability. These results strengthen the link between the conformational dynamics of allergen proteins and their stability during endolysosomal degradation. The presented approach further allows atomistic insights in the conformational ensemble of allergen proteins and provides probability estimates below experimental detection limits.

show abstract

“…The comparison of structure and physicochemical properties of allergens revealed some predictive data related to their allergenic potential. However, for each of them, counter-examples were reported, so that general rules are not applicable [48].…”

Section: Food Processing and Protein Allergenicitymentioning

confidence: 99%

“…However, this proteolytic activity depends on the hydrolytic susceptibility of the allergens, which correlates with their structural properties. For example, β-lactoglobulin and α-lactalbumin, which are compact and globular proteins, are more resistant to gastrointestinal digestion than caseins [48].…”

Section: Fermented Dairy Products and Milk Allergymentioning

confidence: 99%

Allergenicity of Fermented Foods: Emphasis on Seeds Protein-Based Products

Mecherfi

Todorov

Albuquerque

et al. 2020

Foods

Self Cite

View full text Add to dashboard Cite

Food allergy is an IgE-mediated abnormal response to otherwise harmless food proteins, affecting between 5% and 10% of the world preschool children population and 1% to 5% adults. Several physical, chemical, and biotechnological approaches have been used to reduce the allergenicity of food allergens. Fermentation processes that contribute to technological and desirable changes in taste, flavor, digestibility, and texture of food products constitute one of these approaches. Lactic acid bacteria (LAB), used as starter cultures in dairy products, are a subject of increasing interest in fermentation of plant proteins. However, the studies designed to assess the impact of LAB on reduction of allergenicity of seed proteins are at an early stage. This review presents the current knowledge on food fermentation, with a focus on seed proteins that are increasingly used as ingredients, and its impacts on food potential allergenicity.

show abstract

The relevance of a digestibility evaluation in the allergenicity risk assessment of novel proteins. Opinion of a joint initiative of COST action ImpARAS and COST action INFOGEST

Cited by 61 publications

References 187 publications

The pattern of peptides released from dairy and egg proteins is highly dependent on the simulated digestion scenario

The pattern of peptides released from dairy and egg proteins is highly dependent on the simulated digestion scenario

Dynamics Rationalize Proteolytic Susceptibility of the Major Birch Pollen Allergen Bet v 1

Allergenicity of Fermented Foods: Emphasis on Seeds Protein-Based Products

Contact Info

Product

Resources

About