Aarhus University Seal / Aarhus Universitets segl

Immunoglobulins

Antibodies are highly evolved and sophisticated structures that combine specificity recruitment of body´s own defence mechanisms using a set of specialised isotypes.

Hence, for assessment of the physiological and pathophysiological functions of antibodies and for most of the diagnostic and therapeutic approaches the establishment of the entire immunoglobulin is essential. Human, murine and avian immunoglobulins of varying steric requirements and valency can be produced in different pro- and eukaryotic expression systems.

Mediating cellular and humoral effector mechanisms is crucial e.g. in the context of targeting xenobiotic or malignant structures. In allergy, the ratio of specific, high affinity IgE and IgG antibodies are thought to define the status and future outcome of disease.

In contrast to IgG, IgE antibodies are scarcely available and structural and functional characteristics therefore remain difficult to address. Recombinant coupling of specificity with the framework of IgE provides unique handles to dissect clinical relevance and biological function.

In order to activate and improve physiological effector mechanisms different projects aim for dissection of molecular properties of such immunoglobulins by generation of specific antibody isotypes with tailored effector functions.

IgE-mediated hypersensitivity is an excellent example for the fatal interplay of the recognition of highly immunogenic/allergenic epitopes by the still enigmatic isotype IgE and its extraordinarily potent effector mechanisms that can provoke fatal reactions to even minute amounts of antigen.

Our major research focus is the molecular recognition and immunological mechanisms in IgE-mediated hypersensitivities.

Another example are avian antibodies, which represent antecessors and prototypes for antibodies from mammals and can provide insights into basics of molecular recognition. IgY is the major low molecular weight immunoglobulin in oviparous animals. The phylogenetic distance of 250 mio. years and genetic background of birds as well as different biochemical and structural features render them superior in immunoassays, especially those designed to detect molecules in specimens like mammalian blood or serum.