"We can now describe the interaction of this antibody with its target and the conformational changes very accurately. This allows us to understand, how it interferes with the IgE and its specific receptors on the immune cells of the body, which are responsible for releasing histamine in an allergic reaction," said Edzard Spillner, Associate Professor at the Aarhus University.
‘The antibody interacts in a complex biochemical process in the human body by which it prevents the human allergy antibody (IgE) from attaching to cells, thus keeping all allergic symptoms from occurring.’
When exposed to external allergens, an allergic person produces high levels of IgE molecules.
The function of the antibody is that it interferes with binding of IgE to the two specific effector (CD23 and FceRI) on the immune cells, thereby making it impossible for the allergy molecule to bind.
Furthermore, the scientists have observed that the antibody also removes the IgE molecules even after binding to its receptors.
"Once the IgE on immune cells can be eliminated, it doesn't matter that the body produces millions of allergen-specific IgE molecules. When we can remove the trigger, the allergic reaction and symptoms will not occur," Spillner said.
In the laboratory, it took only 15 minutes to disrupt the interaction between the allergy molecules and the immune cells.
The research team has conducted ex vivo experiments with blood cells from patients allergic to birch pollen and insect venom. However, the method can be transferred to virtually all other allergies and asthma, they said.
Because of its chemical structure, the new antibody might be inhaled or swallowed, and these new consumption methods will make easy, cheap and much and more comfortable for the patients to handle.
"It is a so-called single domain antibody which easily produced in processes using only microorganisms. It is also extremely stable, and this provides new opportunities for how the antibody can be administered to patients," Spillner said.