The Bishop Lab’s research on the structure and function of membrane proteins attacks one of the most important and challenging problems in contemporary biochemistry. Their most recent work focuses on an outer membrane enzyme called PagP from pathogenic Gram-negative bacteria. PagP transfers a palmitoyl group from a phospholipid molecule to the lipid A (endotoxin) component of lipopolysaccharide (LPS). This simple modification provides bacterial resistance to host antimicrobial peptides and attenuates the inflammatory response signaled through the human toll-like receptor 4 pathway. By understanding how the structural and dynamic properties of PagP relate to its biological function, the Bishop Lab aims to design inhibitors that are useful for the treatment of infections and to synthesize novel endotoxin antagonists for the treatment of septic shock.
Associate Professor, Biochemistry & Biomedical Sciences