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FARE Blog September 17, 2020

Molecule Identified in Study May Influence Allergies and Reaction Symptoms

Findings from a FARE Investigator may aid the search for food allergy treatments and improved diagnostic tests.

Robert Anthony

Earlier this year, research funded in part by FARE identified and explored a previously unknown immunological difference between people with peanut allergy and people without allergies. The Boston-based research team was led by Robert Anthony, PhD (Harvard Medical School/Massachusetts General Hospital), who received a three-year FARE Investigator in Food Allergy Award in 2017. The study was published in May 2020 in the prestigious journal Nature.

Immune system proteins called IgE antibodies play a key role in allergy. IgE antibodies trigger an allergic reaction when binding an allergen, a protein from outside the body. This binding allows the IgE antibodies to interact with each other on the surface of cells that store histamine and other chemical defenses. Reacting to the allergen as if it were part of an invading germ or parasite, the cells release their chemical payload, causing allergy symptoms. The most severe type of allergic reaction, anaphylaxis, can be life-threatening.

IgE antibodies are a necessary part of the allergic reactions that can result in anaphylaxis. However, some people who make IgE antibodies to a particular food are still able to eat that food without reacting. Why do some people who make food-specific IgE react to the food while others don’t? The answer to this question has the potential to shape innovations in treatment and diagnosis.

Anthony and colleagues discovered that, compared to IgE from individuals with no allergies, IgE from individuals with peanut allergy contained more sialic acid. Sialic acid can be part of a complex sugar structure attached to IgE. These sugars are known to affect the function of some proteins, including some types of antibodies.

In cell cultures and in mice, the research team showed that adding sialic acid made IgE antibodies more effective in triggering histamine release and anaphylaxis, while removing sialic acid made IgE antibodies less effective. These exciting findings have revealed sialic acid as a new possible target for treatments to prevent or minimize anaphylaxis symptoms. The sialic acid content of IgE might also serve as a biomarker to help allergists monitor the effectiveness of a treatment or accurately diagnose food allergy with a more sensitive blood test.

This research will be presented at the 2020 Contains: Courage® Research Retreat, to be held September 21 and 22. This online virtual conference will bring together patient advocates, clinicians, industry representatives and investigators in academia and public service to learn the latest on food allergy biology, treatment, diagnosis, monitoring and prevention, plus FARE’s initiatives to accelerate progress in the field. Dr. Anthony Fauci, the director of the National Institute of Allergy and Infectious Diseases, will make a special guest appearance. For the first time, members of the public are invited to attend this annual event. Learn more and register today.

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