Publication list via PubMed

Our laboratory studies molecular aspects of the complement system, one of the effector mechanisms of the immune system. We are particularly interested in the structure and function of the third component (C3) of the human complement system. We are studying the structural differences of C3 to a highly homologous protein that occurs in the venom in the cobra, called cobra venom factor (CVF). Whereas complement activation in serum is tightly controlled, CVF escapes control and exhaustively activates complement, leading to complement depletion. Complement plays an important biological function in host defense and the immune response; however, inappropriate complement activation is also involved in the pathogenesis of many diseases such as rheumatoid arthritis and reperfusion injury. In these and other diseases therapeutic complement inhibition may be warranted. As CVF is by far the most potent known agent to inhibit complement (by effectively depleting it) our laboratory tries to exploit the structural similarity between CVF and C3 to generate a C3 derivative with CVF-like functions, a protein we have termed “humanized CVF”. Humanized CVF has the potential to become a conceptually novel drug for therapeutic complement inhibition as well as for targeted complement activation for tumor cell killing.

Another research focus of the laboratory is to study the biological function and possible therapeutic potential of natural IgM antibodies against neuroblastoma.