Research Interests:

Cytotoxic T-cells recognize by their T-cell receptors antigenic peptides, which are displayed by Major-Histocompatibilty Class-I complexes (MHC) on surface of cell. These peptides are fragments deriving from intracellular expressed proteins. After their expression a large fraction of proteins is degraded immediately by the proteasome. The proteasomal splicing products are transported to the endoplasmic reticulum, where further trimming and assembling to the MHC-peptide complex occurs. Finally the MHC-peptide complex is translocated via the trans-Golgi compartment to the surface of cell. So far these mechanisms of antigen-processing and –presentation are not fully understood neither under normal nor pathological conditions like malignant transformation of cell. Therefore for many research-purposes it is important to be able to detect a particular peptide in context of the MHC-complex. Naturally only T-cell receptors (TCR) are able to interact with these ligands in such a unique fine specificity. However we generated antibodies recognizing TCR-like manner a particular peptide only when displayed by the MHC complex.

We are primarily using our MHC-peptide-specific antibodies

• to study the influences of malignancy on antigen-processing and –presentation,
• to study the efficacy of antigen-processing and –presentation,
• as a model for the interaction of the T-cell receptor with the MHC-peptide-complex.