Scientists have come a step closer to creating a treatment for peanut allergies by studying the antibodies at work when the food sends the immune system into overdrive.
Allergic reactions happen when the immune system misreads a food protein as a threat. This makes the body create proteins, known as immunoglobulin E (IgE), to attack the allergen. The release of this antibody can cause the potentially fatal symptoms of an allergic reaction, including itching, breathing problems and hives. According to the Food Allergy Research and Education, a nonprofit organization, peanuts are among the most common triggers, alongside eggs, tree nuts, soy, wheat, fish and shellfish.
At the moment, patients with food allergies can treat their condition by taking antihistamines and, in severe cases, carrying an adrenaline shot to administer when they come into contact with their trigger food.
For their study, published in Proceedings of the National Academy of Sciences, scientists recruited 16 patients who were allergic to peanuts. They tested serum from the participants' blood to identify where the IgEs binded with peanut proteins.
Next, the scientists developed inhibitors, enzymes which bind to other enzymes to reduce their activity. Those molecules, which they named covalent heterobivalent inhibitors, were found to stop allergic reactions by stopping IgES from latching on to peanut proteins.
Dr. Basar Bilgicer, co-author of the study and associate professor in the department of chemical and biomolecular engineering at University of Notre Dame, told Newsweek, "My team developed a first-in-class allergen-specific inhibitor that blocks the peanut allergens from being recognized by the patient's immune system. The currently available treatments, such as antihistamines and EpiPen, are to be administered after the allergic reaction has already been initiated. Our approach will inhibit/block the reaction from starting by making the allergens invisible to the patient's immune system."
However, Bilgicer said, a single treatment would not provide a permanent protection from the allergen, and patients would need to take them routinely for constant protection.
"Perhaps the most significant point of the cHBI inhibitor design is that it targets only the immune components that interact with the allergen, and doesn't interfere with any other essential immune system molecules or cells," he said. "This is important because our immune system carries out very important functions that are vital for patient's well-being."
Bilgicer hopes the inhibitors can one day be developed into a treatment to be used in combination with immunotherapy to desensitize the patient's body to peanut proteins.
"We are currently looking into identifying paths to translate our technology to the clinic," he said.
Last year, scientists published research on a newly developed blood test to diagnose peanut allergies thought to be safer and more accurate than methods doctors currently use on patients.
If rolled out, the new test could catch a peanut allergy before patients had to undergo the oral food challenge (OFC), widely considered the gold standard for identifying the condition. The OFC involves giving a patient greater amounts of peanuts incrementally, and must be carried out in a controlled hospital setting due to the risk of potentially life-threatening anaphylactic shock. The work was published in the Journal of Allergy and Clinical Immunology.
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