crystallization of LPS receptors, LBP and Toll

Abstract

Lipopolysaccharide binding protein (LBP) is a 60 kDa acute phase glycoprotein capable of binding to LPS of Gram-negative bacteria and facilitating its interaction with cellular receptors. This process is thought to be of great importance in systemic inflammatory reactions such as septic shock. To study molecular basis of LPS binding and transfer by LBP, we overproduced and purified LBP in Hi5 insect cells using recombinant baculoviruses. The purified LBP was crystallized by vapor diffusion technique. The LBP crystals diffracted x-ray to 2.8Å resolution and the structure determination is under progress. The crystal structure of LBP will be used as a key of drug for use in the treatment of Gram-negative bacterial sepsis.