X-ray Crystallography and Biophysical Characterization of
Proteins Involved in Infectious Disease
Our research investigates the three-dimensional structure and molecular mechanism of proteins central to infectious disease using crystallographic and biophysical methods. We currently are investigating proteins that mediate host-pathogen interactions involving the human immune system by employing X-ray crystallography to determine high-resolution structures of virulence factors from pathogenic bacteria. We are studying effectors that transform benign environmental bacteria into dangerous human pathogens. Our recent efforts have focused on in two primary areas: pore-forming toxins and biofilm-related proteins. This information will not only provide insight into the pathology of opportunistic human pathogens, but also aid in the engineering of agents for a host of therapeutic and biotechnological applications. These studies seek to delineate the structural underpinnings that allow pathogens to infect human hosts.
Vibrio cholerae cytolysin (PDB:3O44)
Bap1 Biofilm Matrix Protein from Vibrio cholerae (PDB:6MLT)