We seek to understand the structural basis of virus maturation and virus assembly. We are particularly interested to investigate the role of cellular proteins in the transport of viral effectors and in the membranlocalization in cholesterol- rich microdomains, so called lipid rafts. For murinen g-retroviruses (e.g. mouse leukemia virus) it has been shown that the raft associated protein caveolin-1 plays a crucial role in the membrane attachment. This process appears to be guided by the matrix protein (MA) and homologous proteins from unrelated viruses display a similar behavior.

In this project, recombinant caveolin-1 will be produced E. coli and functionally reconstituted in phospholipids. It is expected to obtain sufficient isotopically labeled yields to investigate the species-specific interactions of Cav-1 with MA by NMR-spectroscopy and other biophysical techniques. The knowledge of the structural determinants is of crucial importance to understand viral host-specificity, and for the development of molecular targets for antiviral therapies.

The successfull candidate will be introduced into all essential molecular biological and protein biochemical techniques. The obtained products will be first characterized using biophysical techniques like biacore, fluorescence, CD-spectroscopy, fourier transform infrared and light scattering. The functionality of the obtained complexes will be investiagetd using tissue culture techniques in collaboration with the laboratory of molekular Biotechnology (Dr. Manfred Wirth).