Allergic reactions, including allergic rhinitis, asthma, drug allergies, etc., cause trouble for hundreds of millions of people worldwide. Recently, the reporter learned from Shenzhen Academy of Medical Sciences that the specially appointed researcher Su Qiang, together with researchers from West Lake University, has discovered the key role of immune receptor morphological changes in allergic reactions through in-depth research on allergy mechanisms, which is expected to provide new ideas for the development of allergy drugs. The relevant paper was published online on the evening of October 23rd Beijing time in the internationally authoritative journal Nature. Previous studies have found that when the antibody for allergic reactions, core immunoglobulin IgE, binds to high affinity receptors, it activates mast cells and eosinophils, leading to allergic reactions such as vasodilation and bronchoconstriction. In severe cases, it can cause systemic anaphylactic shock. Therefore, in the past, drug design for allergies in clinical practice mainly focused on how to block the binding of antibodies to receptors, with a focus on inhibiting histamine release, "said Su Qiang. However, due to the weak research on the transmembrane region of receptors, how the binding of antibodies to immune receptors activates allergy related signaling pathways and the specific molecular mechanisms behind it are still unclear, which also limits the approach to clinical drug development. In response, the research team utilized cryo electron microscopy technology and combined in vitro biochemical and in vivo cell experiments to analyze protein structures and reveal the dynamic mechanisms behind allergic reactions. Researchers have found that when antibodies bind to immune receptors, the morphology of the immune receptors changes from dimers to monomers. This morphological change leads to the exposure of protein sites in related signaling pathways, which in turn activates downstream signaling pathways and causes allergies. Su Qiang said that now that this dynamic process has been revealed, in the future, it can be considered to keep the receptor in a dimeric form and prevent it from changing, so that the protein sites of related signaling pathways will not be exposed. Even if allergens trigger the binding of antibodies to immune receptors, the signaling pathway of allergies cannot be activated, and allergic reactions will not occur. Through this study, the framework of allergy mechanisms has become clearer and more accurate. Our next step is to develop a 'molecular glue' that keeps the morphology of immune receptors fixed, allowing patients to effectively avoid allergies Su Qiang said. (New Society)