“Crystallography enables us to see a single atom in the highest resolution now in existence. Having this detailed, structured image is a significant advantage in combating disease because it’s easier to stop what you can see.” – Dirk Zajonc, Ph.D.Dr. Zajonc received his M. Sc from the University of Erlangen-Nurembergin 1998 and his Ph. D. in biochemistry in 2001, for his work on fatty acid elongation and sphingolipid metabolism in bakers yeast.
For his postdoctoral training, Dr. Zajonc joined the lab of Ian A. Wilson at the Scripps Research Institute in 2001. He then became interested in the structural aspects of how lipids can serve as immunogens and how they can be presented and recognized by the immune system. He used x-ray crystallography to determine various structures of CD1 immune receptors bound to different glycolipids and lipopeptides.
Dr. Zajonc joined LIAI in 2005 as an Assistant Member in the Division of Cellular Biology, where he will continue to work on various structural aspects of immune recognition.
Our group is primarily interested in the structural basis of immune recognition of lipids, how these lipids can modulate an immune response, or how lipid modification of immunologically important proteins can affect immune signalling. In addition, we want to understand on a molecular level, how various lipids from pathogenic organisms, such as Mycobacterium tuberculosis, are synthesized. These insights will eventually lead to the development of chemotherapeutic agents against tuberculosis and other diseases.
Crystal structures of mouse CD1d-iGb3 complex and its cognate Valpha14 T cell receptor suggest a model for duel recognition of foreign and self glycolipids.