Area of Doctoral Study: Biochemistry
Undergraduate Institution: University of Maryland, College Park
Research Advisor: James P. Nataro and Jim Kaper
Current Position: Instructor of Pediatrics and Associate in Medicine, Division of Infectious Diseases, Children’s Hospital Boston
Description of Research
EspP is an extracellular serine protease that is encoded by enterohemorrhagic Escherichia coli (EHEC). It has been shown to cleave coagulation factor V which may help explain the mechanism by which it causes the characteristic hemmorrhagic colitis (Brunder et al., 1997). Additionally, it has been classified as a member of the SPATE (Serine protease autotransporters of Enterobacteriaceae) family. This family is unique in its mechanism of exporting the proteases from the periplasmic space to the extracellular space. They are hypothesized to create a barrel in the outer membrane and permit the passenger domain to go through and be cleaved, releasing it into the extracellular space. The project involves studying the structure and function relationship of this secreted protein. This should include the definition of various domains as well as structural and mutagenesis studies aimed at understanding these domains. When completed, these studies should yield information regarding the functional mechanisms of EspP as well as providing a clearer understanding of its possible use as a biotechnology tool for vaccine development and therapeutic purposes.