The goal of this program is to elucidate three dimensional structures of bacterial surface proteins and their receptor complexes.  Structural information allows us to understand the interaction of these proteins with their receptors and their role in virulence and pathogenesis.  This knowledge can be used for designing vaccines and therapeutic tools.  One of the projects in this program aims at defining surface epitopes on the pneumococcal surface protein A of Streptococcus pneumonia, which is a major virulence factor and a vaccine candidate and elucidating the molecular basis of its recognition and binding to lactoferrin.  In the second project in this program we are studying the three dimensional structure of a major virulence factor, Psn, of Yersinia pestis, the causative agent of bubonic plague.  This outer membrane protein is a dual receptor for the siderophore, yersiniabactin and for the bacteriocin, pesticin.

Other bacterial surface protein crystals that have been studied in our laboratory:

	E. coli NAD synthetase:
	Staphylokinase: