New research on allergy treatment

New research on allergy treatment

April 08, 2015 Source: Bio Valley

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April 7th, 2015 / Bio Valley BIOON / -- Allergic reactions are a small illness that everyone can get more or less. At its root, allergic reactions are mediated by a specific class of immunoglobulins (IgE) in the body. IgE Tender Consolidation specifically recognizes a wide variety of allergens in the environment and triggers allergic effects through the FcεR1 receptor on the surface of the mast cells interspersed between tissues.

For IgG, the glycosylation characteristics of its protein surface can affect its final biological function, but there is much less research on IgE. Recently, Robert M. Anthony, a research group from the Harvard Medical School and the Massachusetts General Hospital Immunization and Inflammatory Diseases Center, published a study in this journal in JEM.
First, the authors designed the following experiments to collect IgE antibodies: they injected OVA or other common food allergens and alum adjuvants into mice. Thereafter, the mouse serum is extracted and further processed to filter out IgG in the serum. As a result, most of the serum contains antibodies of the IgE type. Thereafter, the authors digested the N-linked oligosaccharide chain on these polyclonal antibodies by in vitro enzymatic treatment to obtain an aglycosylated IgE antibody. Subsequently, the authors injected these antibodies into the vicinity of the mouse's ears by subcutaneous injection (a common model for inducing allergic reactions). The results showed that IgE antibodies that did not undergo a digestive response caused a strong allergic reaction: rupture of the blood vessels and blueness of the eyes. In contrast, the deglycosylated IgE antibody did not cause the above reaction. Thereafter, the authors performed the same experiment using OVA-specific IgE, and the results were the same as above. The results of this experiment demonstrate that glycosylation of the IgE surface plays an important role in its ability to mediate allergic reactions.
In order to determine which site of glycosylation is important for the function of IgE, the authors prepared a series of different glycosylation deletion mutants by mutation (asparagine-glutamine). Later, through the same in vivo induction experiments, the authors found that glycosylation in the IgE Cε3 domain is decisive for its induction of allergic reactions. Since the Cε3 domain has two asparagine sites inside, it is 361 and 384, respectively. The authors mutated two loci and induced them in vivo. The results showed that both the N384Q mutation and the wild type caused a strong allergic reaction, while the N361Q mutation lost this effect. This experimental result indicates that glycosylation at the 384 site is important for the function of IgE.

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