I studied Physics Engineering at Politecnico di Milano (Milano, Italy), where I earned a bachelor’s degree followed by a master’s degree. Both of them consisted mainly of solid state physics classes, with a particular focus on semiconductors (for electronics and photonics application) and magnetic nanostructures. My first experience in research was at the European Synchrotron Radiation Facility (Grenoble, France), where I spent 10 months working as a trainee for my master thesis project.
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Viruses have evolved ingenious mechanisms to reprogram the environment of infected cells to best suit their replication, and understanding how viruses achieve this is key to developing the next generation of anti-viral therapies. This project brings together two world-leading research institutes to combine cutting-edge super-resolution fluorescence microscopy, cryo X-ray tomography (cryoXT), biochemistry and cell biology approaches to probe the molecular details of how herpesviruses remodel membranes during infection.
Herpesviruses are highly prevalent human and animal pathogens that cause serious diseases. These viruses dramatically remodel the endomembrane system of infected cells to efficiently produce membrane-wrapped infectious progeny. We seek to determine the molecular pathways that stimulate envelopment of the human herpesviruses. Previous work in our laboratories has identified conserved viral protein complexes required for efficient membrane wrapping of nascent virus particles. However, the details of the envelopment process and the stages involving these complexes remains unclear. We will use super-resolution fluorescence microscopy and cryoXT to unravel the spatiotemporal dynamics of virus wrapping in cells infected with wild-type or mutant herpesvirus strains. Correlative fluorescence microscopy and cryoXT will allow us to identify specific virus proteins at sites of virion assembly and capture whole-cell images of the envelopment process at nanometer resolution. By systematically investigating defects in virus envelopment across a panel of genetically-engineered mutant strains of HSV-1 we will be able to dissect the specific roles played by each of the conserved protein complexes that promote virus envelopment.
In addition to uncovering the roles of particular viral proteins during envelopment, host factor requirement and function will be investigated. Our laboratories have identified a number of cellular proteins required for efficient virus assembly. We will investigate these interactions biochemically and use infection-based cellular assays (of wild type or CRISPR/Cas9 genome edited human cells) to probe how these host proteins contribute to virus assembly.
Applications to this studentship will open in early 2018.
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