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Storage Protein And Food Allergies: Diagnosis And Risks

Diagnosis And Risks Of Different Allergens

Food allergy is a current and growing problem, given the broad spectrum of clinical manifestations that can range from milder to potentially fatal anaphylactic shock. Specifically, in the face of sensitization to storage proteins, an accurate diagnosis by an expert allergist is essential since it is a condition that can cause severe reactions, such as that caused by allergy to peanuts in children. So here is a helpful overview to understand.

The Advantages Of Molecular Diagnostics

Thanks to the latest molecular biology techniques, it has been possible to significantly expand the knowledge of allergens and their role in food allergies. The diagnostics based on classic allergenic extracts can only identify the allergenic source, therefore identifying the fruit responsible for the reaction, but does not allow placing the molecular entity accountable for the sensitization (LTP, PR-10, or deposition proteins). 

The use of single purified molecules to define the patient’s allergen profile, therefore, constitutes a crucial diagnostic refinement and affects the prognosis and therapeutic indications. This system allows informing the patient about the level of risk that it involves any awareness, more significant if developed for deposit proteins compared, for example, to raising awareness for the apple pr-10, which generally causes a simple “syndrome Allergic oral,” characterized by itching at the level of the oral cavity and edema of the lips. 

Deposit Proteins And Their Role In Allergies

Among the allergens, the storage proteins are the most present in the seeds and dried fruit with shell, albeit in the latter, next to a minimal concentration of proteins Bet V 1 counterparts, profiles, and LTP. The family of deposit proteins consists of various proteins belonging to two super famous proteins: prolamins and lupines. Both have a remarkably stable chemical structure to heat and protease, so they are more resistant to cooking and more difficult to digest. Their definition is often based on the sedimentation coefficient: the 7S and 11s globulins belong to the lupines, the 2S albumins, and the lipid transfer proteins belong to the prolamins.

The former is contained in the seeds of many plants and includes the globulins of soy, Arachidic, Ana cardo, and walnut. The lupines also belong to the legumin of the hazelnut and the almond, whose roasting does not affect the allergenic ability and the danger of triggering severe reactions. In determining the risk of developing symptoms, IgE levels have an essential role, while the severity of the same seems to be influenced by co-sensitization to different deposit proteins. For this reason, awareness of the deposit proteins is an essential index of a possible systemic severe reaction. It must be reported to the patient by warning it of potential risks.

As for the prolamins, however, this type of deposit protein is present in wheat

It is distinguished in numerous allergens, such as the Omega 5 -agina (Tri to 19), head of the paintings of anaphylaxis related to physical exercise (food-dependent exercise-induced anaphylaxis). This type of allergy, which causes severe clinical pictures, is fortunately relatively rare. In the case of the cereals’ prolamins of the grains, unlike the cupines, it is shown that cooking can consistently influence the level of allergenicity. Speaking of prolamins, it is essential to indicate that 2s albumins can also cause an allergic reaction by inhalation. These allergens are found in peanuts, yellow mustard, walnut, sesame, almond, sunflower seeds, soybeans, and chickpeas. These proteins are highly resistant to heat and digestion. 


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