The ability of bacterial pathogens to invade and survive within the cells of a human host is governed by the interplay between host and bacterial factors. Under these conditions, both host and pathogen generate multiple mediators that, through interactions with other proteinous factors alter the intercellular host environment. These interactions govern the development of disease and are largely mediated by the physical association of proteins and the generation of protein complexes. Currently, our understanding of protein complexes and the remodeling of complexes in response to certain bacterial pathogens such as the leading foodborne cause of gastroenteritis, Campylobacter jejuni, are incomplete. This incomplete understanding of the dynamic changes in the host in response to bacterial infection is due multiple shortcomings associated with traditional approaches for investigating protein interactions.
Ideally, to better understand how C. jejuni interacts and survives in the human host, a greater understanding of the dynamics of protein complexes are required. In his analysis, Dr. Scott aims to understand the molecular changes in response to C. jejuni infection and to further develop the use of protein correlation profiling to study protein interactions.
Recently, it was demonstrated that the use of size exclusion chromatography, metabolic protein labeling and mass spectrometry provided an ideal platform to study the interaction of complexes under multiple conditions (Kristensen et al, Nat. Meth. 2012). By examining the C. jejuni infection of human cells through these imagings techniques, the mechanism by which this pathogen develops can be further understood.
The information garnered through Dr. Scott’s research can be incorporated into studies aimed at using traditional targeted approaches to understand how protein interactions contribute to changes in the host as a result of bacterial agents.