Helicobacter pylori is the primary cause of stomach cancer, which is the third leading cause of cancer deaths worldwide. The helical shape of the bacterium is necessary for efficient stomach colonization. Thus, if researchers can understand the mechanisms by which H. pylori achieves its shape, they may be able to identify novel therapeutic strategies.
Previously, Fred Hutchinson Cancer Center faculty member Dr. Nina Salama and her team used genetic screening to identify a set of proteins that, when deleted, resulted in distinctly non-helical cell shapes.
Salama and her team wanted to find other proteins that interact with one of the shape-forming proteins they’d identified in their earlier work, called Csd5. Mass spectrometry-based proteomics is the primary technology for identifying protein-protein interactions. But the Salama Lab is not well-versed in the complexities of the technology or how to obtain optimal results.
The Proteomics & Metabolomics shared resource at Fred Hutch offered the technological expertise the Salama Lab needed to answer their questions about Csd5. Salama’s team worked in conjunction with the core to design and carry out immunoprecipitation mass spectrometry, or IP-MS, experiments using Csd5 fusion constructs to identify proteins that interact with Csd5. The core provided high-resolution mass spectrometry experiments and data analysis to identify protein-protein interactors. This research would not have possible without access to an experienced proteomics facility.