My project

In Gram-positive bacteria, which have no outer membrane, the cell wall represents a scaffold for the display of a large variety of proteins. The aim of this project is study the mechanisms underpinning protein surface display to understand how pathogens interact with their environment. We will focus on a model protein domain called WxL conserved across bacteria. WxL domains have originally been described in a protein contributing to the virulence of the nosocomial pathogen Enterococcus faecalis.

This project will involve a wide range of techniques including protein purification, bacterial cell wall analysis by HPLC and mass spectrometry as well as state of the art approaches to study protein-cell wall interaction. A key asset for this work will be the access to Isothermal Titration Calorimetry (ITC) and thermophoresis equipment available Department of Molecular Biology and Biotechnology within the MBB department. We will also analyze the subcellular localization of cell surface proteins containing WxL domains by deconvolution fluorescence microscopy in live bacteria expressing fluorescent proteins. Recombinant WxL domains will also be labelled with fluorophores and used as probes to map their binding sites on the bacterial cell surface by super resolution microscopy at a nanometer scale.

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