Max-Planck-Scientists decipher central protein complex in the human immune system / Relevance for future therapies in allergies, autoimmune diseases and transplantation medicine
A key building block of the human immune system was identified up to the atomic detail using the method of x-ray crystallography by scientists of the Max-Planck-Institute for Biochemistry in Martinsried/Germany (Nature, 20. July 2000, S. 267-273). The protein complex, a mediator between the soluble and cellular compounds of the immune components in the blood, consists of an antibody and its respective receptor. Their dialogue in the immune system ensures that pathogenic germs which were previously labeled with antibodies are removed by receptor-equipped immune cells, eg macrophages. The identification of the structure and of the exact location of the interaction site between both proteins opens new possibilities not only for the therapy of diseases like allergies or autoimmune diseases, but also in the field of transplantation medicine.
The most important weapon in the defense of diseases in the human organism are Y-shaped antibodies, the so-called immunoglobulins (Ig). Many quintillions of antibodies with more than a trillion different specificities are found in the blood of the human body. These subdivide themselves - as within all mammals - into five different antibody types: IgM, IgG, IgA, IgD and IgE. Every class has its own particular characteristics that makes it possible to adopt a certain defense function. IgA for example, can be transported through the uppermost layer of the skin and is found in saliva, sweat and tears.
The well investigated immunoglobulin IgG is, with 80 percent, the most abundant antibody class in the circulation.
It easily passes through walls of blood vessels or the placental barrier and confers, by this, passive immun
Contact: Peter Sondermann