Scientists have analyzed how the intracellular pathogen Salmonella enterica secretes proteins to survive and thrive in infected cells. Using a novel approach, which for the first time allows scientists to study which host cell proteins are targeted by the pathogen, the scientists revealed new insights into how Salmonella hijacks the cell´s cholesterol supplies, and how it rewires cellular transport processes to promote its own survival.
To find these enigmatic protein interactions, the EMBL scientists genetically engineered 32 Salmonella strains by adding identification tags to individual Salmonella proteins -- earmarking one protein in each bacterial strain. The identification tags act like a handle the scientists can grab in their experiments. This approach of modifying the effector proteins directly in their host is a breakthrough. It enables researchers to capture the bacterial proteins after they have been secreted into infected cells, and to pull them out along with any host cell proteins that are bound to them. These interacting proteins are then identified using a technique called mass spectrometry.
See:
Philipp Walch, Joel Selkrig, Leigh A. Knodler, Mandy Rettel, Frank Stein, Keith Fernandez, Cristina Viéitez, Clément M. Potel, Karoline Scholzen, Matthias Geyer, Klemens Rottner, Olivia Steele-Mortimer, Mikhail M. Savitski, David W. Holden, Athanasios Typas. Global mapping of Salmonella enterica-host protein-protein interactions during infection. Cell Host & Microbe, 2021; DOI: 10.1016/j.chom.2021.06.004
Posted by Dr. Tim Sandle, Pharmaceutical Microbiology Resources (http://www.pharmamicroresources.com/)
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