| |
 |
|
 |
Jorge Velarde
Area of Doctoral Study:Biochemistry
Research Advisor: James P. Nataro, and Jim Kaper
Description of Doctoral 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. The 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.
|
|
